891f_f679
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 20.0 | 13.4 |
| 0.002 | 34.3 | 20.0 |
| 0.005 | 60.0 | 28.6 |
| 0.010 | 80.0 | 33.4 |
| 0.020 | 96.0 | 36.4 |
| 0.050 | 109.1 | 38.5 |
| 0.100 | 114.3 | 39.3 |
| 0.200 | 117.1 | 39.7 |
| 0.500 | 118.9 | 39.9 |
| 1.000 | 119.5 | 40.0 |
| 2.000 | 119.8 | 40.0 |
| 5.000 | 119.9 | 40.0 |
| 10.000 | 120.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Incorrect para-competitive Incorrect quasi-competitive Incorrect un-competitive Correct MCdbc1_58f3
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 12.8 | 13.4 |
| 0.002 | 23.4 | 22.9 |
| 0.005 | 46.7 | 40.0 |
| 0.010 | 70.0 | 53.4 |
| 0.020 | 93.4 | 64.0 |
| 0.050 | 116.7 | 72.8 |
| 0.100 | 127.3 | 76.2 |
| 0.200 | 133.4 | 78.1 |
| 0.500 | 137.3 | 79.3 |
| 1.000 | 138.7 | 79.7 |
| 2.000 | 139.4 | 79.9 |
| 5.000 | 139.8 | 80.0 |
| 10.000 | 139.9 | 80.0 |
| 20.000 | 140.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect extra-competitive Incorrect mega-competitive Incorrect non-competitive Incorrect un-competitive Correct MCf1c0_d868
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 20.0 | 0.1 |
| 0.002 | 34.3 | 0.1 |
| 0.005 | 60.0 | 0.2 |
| 0.010 | 80.0 | 0.3 |
| 0.020 | 96.0 | 0.5 |
| 0.050 | 109.1 | 1.2 |
| 0.100 | 114.3 | 2.4 |
| 0.200 | 117.1 | 4.7 |
| 0.500 | 118.9 | 11.0 |
| 1.000 | 119.5 | 20.0 |
| 2.000 | 119.8 | 34.3 |
| 5.000 | 119.9 | 60.0 |
| 10.000 | 120.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct hetero-competitive Incorrect hyper-competitive Incorrect non-competitive Incorrect un-competitive Incorrect MCb7cb_d710
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 2.0 | 1.9 |
| 0.002 | 3.7 | 3.4 |
| 0.005 | 8.0 | 6.7 |
| 0.010 | 13.4 | 10.0 |
| 0.020 | 20.0 | 13.4 |
| 0.050 | 28.6 | 16.7 |
| 0.100 | 33.4 | 18.2 |
| 0.200 | 36.4 | 19.1 |
| 0.500 | 38.5 | 19.7 |
| 1.000 | 39.3 | 19.9 |
| 2.000 | 39.7 | 20.0 |
| 5.000 | 39.9 | 20.0 |
| 10.000 | 40.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect eco-competitive Incorrect non-competitive Incorrect ultra-competitive Incorrect un-competitive Correct MC9d6d_62b1
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 23.4 | 13.4 |
| 0.002 | 40.0 | 22.9 |
| 0.005 | 70.0 | 40.0 |
| 0.010 | 93.4 | 53.4 |
| 0.020 | 112.0 | 64.0 |
| 0.050 | 127.3 | 72.8 |
| 0.100 | 133.4 | 76.2 |
| 0.200 | 136.6 | 78.1 |
| 0.500 | 138.7 | 79.3 |
| 1.000 | 139.4 | 79.7 |
| 2.000 | 139.7 | 79.9 |
| 5.000 | 139.9 | 80.0 |
| 10.000 | 140.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Correct para-competitive Incorrect proto-competitive Incorrect un-competitive Incorrect MC5861_6a4b
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 16.7 | 2.0 |
| 0.002 | 28.6 | 3.9 |
| 0.005 | 50.0 | 9.1 |
| 0.010 | 66.7 | 16.7 |
| 0.020 | 80.0 | 28.6 |
| 0.050 | 91.0 | 50.0 |
| 0.100 | 95.3 | 66.7 |
| 0.200 | 97.6 | 80.0 |
| 0.500 | 99.1 | 91.0 |
| 1.000 | 99.6 | 95.3 |
| 2.000 | 99.8 | 97.6 |
| 5.000 | 100.0 | 99.1 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
anti-competitive Incorrect competitive Correct non-competitive Incorrect oligo-competitive Incorrect un-competitive Incorrect MCb598_12ba
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 1.6 | 0.4 |
| 0.002 | 3.1 | 0.8 |
| 0.005 | 7.3 | 1.9 |
| 0.010 | 13.4 | 3.4 |
| 0.020 | 22.9 | 5.8 |
| 0.050 | 40.0 | 10.0 |
| 0.100 | 53.4 | 13.4 |
| 0.200 | 64.0 | 16.0 |
| 0.500 | 72.8 | 18.2 |
| 1.000 | 76.2 | 19.1 |
| 2.000 | 78.1 | 19.6 |
| 5.000 | 79.3 | 19.9 |
| 10.000 | 79.7 | 20.0 |
| 20.000 | 79.9 | 20.0 |
| 50.000 | 80.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Correct ortho-competitive Incorrect self-competitive Incorrect un-competitive Incorrect MC8ba9_1a74
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 3.2 | 0.8 |
| 0.002 | 6.2 | 1.6 |
| 0.005 | 14.6 | 4.0 |
| 0.010 | 26.7 | 7.7 |
| 0.020 | 45.8 | 14.6 |
| 0.050 | 80.0 | 32.0 |
| 0.100 | 106.7 | 53.4 |
| 0.200 | 128.0 | 80.0 |
| 0.500 | 145.5 | 114.3 |
| 1.000 | 152.4 | 133.4 |
| 2.000 | 156.1 | 145.5 |
| 5.000 | 158.5 | 153.9 |
| 10.000 | 159.3 | 156.9 |
| 20.000 | 159.7 | 158.5 |
| 50.000 | 159.9 | 159.4 |
| 100.000 | 160.0 | 159.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct non-competitive Incorrect poly-competitive Incorrect post-competitive Incorrect un-competitive Incorrect MC34c0_800a
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 13.4 | 0.1 |
| 0.002 | 20.0 | 0.1 |
| 0.005 | 28.6 | 0.1 |
| 0.010 | 33.4 | 0.1 |
| 0.020 | 36.4 | 0.2 |
| 0.050 | 38.5 | 0.4 |
| 0.100 | 39.3 | 0.8 |
| 0.200 | 39.7 | 1.6 |
| 0.500 | 39.9 | 3.7 |
| 1.000 | 40.0 | 6.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct homo-competitive Incorrect non-competitive Incorrect omni-competitive Incorrect un-competitive Incorrect MC0ae2_a173
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 53.4 | 40.0 |
| 0.002 | 80.0 | 53.4 |
| 0.005 | 114.3 | 66.7 |
| 0.010 | 133.4 | 72.8 |
| 0.020 | 145.5 | 76.2 |
| 0.050 | 153.9 | 78.5 |
| 0.100 | 156.9 | 79.3 |
| 0.200 | 158.5 | 79.7 |
| 0.500 | 159.4 | 79.9 |
| 1.000 | 159.7 | 80.0 |
| 2.000 | 159.9 | 80.0 |
| 5.000 | 160.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect homo-competitive Incorrect non-competitive Incorrect proto-competitive Incorrect un-competitive Correct MCdd33_0b9e
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 3.6 | 3.9 |
| 0.002 | 7.0 | 7.3 |
| 0.005 | 16.4 | 16.0 |
| 0.010 | 30.0 | 26.7 |
| 0.020 | 51.5 | 40.0 |
| 0.050 | 90.0 | 57.2 |
| 0.100 | 120.0 | 66.7 |
| 0.200 | 144.0 | 72.8 |
| 0.500 | 163.7 | 77.0 |
| 1.000 | 171.5 | 78.5 |
| 2.000 | 175.7 | 79.3 |
| 5.000 | 178.3 | 79.7 |
| 10.000 | 179.2 | 79.9 |
| 20.000 | 179.6 | 80.0 |
| 50.000 | 179.9 | 80.0 |
| 100.000 | 180.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect dis-competitive Incorrect hetero-competitive Incorrect non-competitive Incorrect un-competitive Correct MCbee9_15b4
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 3.6 | 0.1 |
| 0.002 | 7.0 | 0.1 |
| 0.005 | 16.4 | 0.2 |
| 0.010 | 30.0 | 0.4 |
| 0.020 | 51.5 | 0.8 |
| 0.050 | 90.0 | 1.8 |
| 0.100 | 120.0 | 3.6 |
| 0.200 | 144.0 | 7.0 |
| 0.500 | 163.7 | 16.4 |
| 1.000 | 171.5 | 30.0 |
| 2.000 | 175.7 | 51.5 |
| 5.000 | 178.3 | 90.0 |
| 10.000 | 179.2 | 120.0 |
| 20.000 | 179.6 | 144.0 |
| 50.000 | 179.9 | 163.7 |
| 100.000 | 180.0 | 171.5 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct non-competitive Incorrect pseudo-competitive Incorrect supra-competitive Incorrect un-competitive Incorrect MCe5f8_47e2
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 20.0 | 5.5 |
| 0.002 | 30.0 | 10.0 |
| 0.005 | 42.9 | 20.0 |
| 0.010 | 50.0 | 30.0 |
| 0.020 | 54.6 | 40.0 |
| 0.050 | 57.7 | 50.0 |
| 0.100 | 58.9 | 54.6 |
| 0.200 | 59.5 | 57.2 |
| 0.500 | 59.8 | 58.9 |
| 1.000 | 59.9 | 59.5 |
| 2.000 | 60.0 | 59.8 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct intra-competitive Incorrect non-competitive Incorrect oligo-competitive Incorrect un-competitive Incorrect MC313a_06fa
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 13.4 | 10.0 |
| 0.002 | 20.0 | 13.4 |
| 0.005 | 28.6 | 16.7 |
| 0.010 | 33.4 | 18.2 |
| 0.020 | 36.4 | 19.1 |
| 0.050 | 38.5 | 19.7 |
| 0.100 | 39.3 | 19.9 |
| 0.200 | 39.7 | 20.0 |
| 0.500 | 39.9 | 20.0 |
| 1.000 | 40.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect contra-competitive Incorrect non-competitive Incorrect quasi-competitive Incorrect un-competitive Correct MC1188_e2f0
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 26.7 | 1.6 |
| 0.002 | 40.0 | 3.1 |
| 0.005 | 57.2 | 7.3 |
| 0.010 | 66.7 | 13.4 |
| 0.020 | 72.8 | 22.9 |
| 0.050 | 77.0 | 40.0 |
| 0.100 | 78.5 | 53.4 |
| 0.200 | 79.3 | 64.0 |
| 0.500 | 79.7 | 72.8 |
| 1.000 | 79.9 | 76.2 |
| 2.000 | 80.0 | 78.1 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct iso-competitive Incorrect non-competitive Incorrect semi-competitive Incorrect un-competitive Incorrect MC0d0c_87c6
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 11.0 | 10.0 |
| 0.002 | 20.0 | 17.2 |
| 0.005 | 40.0 | 30.0 |
| 0.010 | 60.0 | 40.0 |
| 0.020 | 80.0 | 48.0 |
| 0.050 | 100.0 | 54.6 |
| 0.100 | 109.1 | 57.2 |
| 0.200 | 114.3 | 58.6 |
| 0.500 | 117.7 | 59.5 |
| 1.000 | 118.9 | 59.8 |
| 2.000 | 119.5 | 59.9 |
| 5.000 | 119.8 | 60.0 |
| 10.000 | 119.9 | 60.0 |
| 20.000 | 120.0 | 60.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect inter-competitive Incorrect non-competitive Incorrect semi-competitive Incorrect un-competitive Correct MC853e_0ba3
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 14.6 | 12.8 |
| 0.002 | 26.7 | 23.4 |
| 0.005 | 53.4 | 46.7 |
| 0.010 | 80.0 | 70.0 |
| 0.020 | 106.7 | 93.4 |
| 0.050 | 133.4 | 116.7 |
| 0.100 | 145.5 | 127.3 |
| 0.200 | 152.4 | 133.4 |
| 0.500 | 156.9 | 137.3 |
| 1.000 | 158.5 | 138.7 |
| 2.000 | 159.3 | 139.4 |
| 5.000 | 159.7 | 139.8 |
| 10.000 | 159.9 | 139.9 |
| 20.000 | 160.0 | 140.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect extra-competitive Incorrect hyper-competitive Incorrect non-competitive Correct un-competitive Incorrect MCcac7_dead
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 10.0 | 6.7 |
| 0.002 | 17.2 | 10.0 |
| 0.005 | 30.0 | 14.3 |
| 0.010 | 40.0 | 16.7 |
| 0.020 | 48.0 | 18.2 |
| 0.050 | 54.6 | 19.3 |
| 0.100 | 57.2 | 19.7 |
| 0.200 | 58.6 | 19.9 |
| 0.500 | 59.5 | 20.0 |
| 1.000 | 59.8 | 20.0 |
| 2.000 | 59.9 | 20.0 |
| 5.000 | 60.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
auto-competitive Incorrect competitive Incorrect non-competitive Incorrect poly-competitive Incorrect un-competitive Correct MC4b16_2931
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 18.2 | 9.6 |
| 0.002 | 33.4 | 18.2 |
| 0.005 | 66.7 | 40.0 |
| 0.010 | 100.0 | 66.7 |
| 0.020 | 133.4 | 100.0 |
| 0.050 | 166.7 | 142.9 |
| 0.100 | 181.9 | 166.7 |
| 0.200 | 190.5 | 181.9 |
| 0.500 | 196.1 | 192.4 |
| 1.000 | 198.1 | 196.1 |
| 2.000 | 199.1 | 198.1 |
| 5.000 | 199.7 | 199.3 |
| 10.000 | 199.9 | 199.7 |
| 20.000 | 200.0 | 199.9 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct non-competitive Incorrect ortho-competitive Incorrect semi-competitive Incorrect un-competitive Incorrect MC43ea_7316
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 3.9 | 0.1 |
| 0.002 | 7.3 | 0.2 |
| 0.005 | 16.0 | 0.4 |
| 0.010 | 26.7 | 0.8 |
| 0.020 | 40.0 | 1.6 |
| 0.050 | 57.2 | 3.9 |
| 0.100 | 66.7 | 7.3 |
| 0.200 | 72.8 | 13.4 |
| 0.500 | 77.0 | 26.7 |
| 1.000 | 78.5 | 40.0 |
| 2.000 | 79.3 | 53.4 |
| 5.000 | 79.7 | 66.7 |
| 10.000 | 79.9 | 72.8 |
| 20.000 | 80.0 | 76.2 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct intra-competitive Incorrect non-competitive Incorrect pre-competitive Incorrect un-competitive Incorrect MC912d_70ae
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 40.0 | 30.0 |
| 0.002 | 60.0 | 40.0 |
| 0.005 | 85.8 | 50.0 |
| 0.010 | 100.0 | 54.6 |
| 0.020 | 109.1 | 57.2 |
| 0.050 | 115.4 | 58.9 |
| 0.100 | 117.7 | 59.5 |
| 0.200 | 118.9 | 59.8 |
| 0.500 | 119.6 | 59.9 |
| 1.000 | 119.8 | 60.0 |
| 2.000 | 119.9 | 60.0 |
| 5.000 | 120.0 | 60.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect intra-competitive Incorrect non-competitive Incorrect para-competitive Incorrect un-competitive Correct MC8268_ad0f
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 20.0 | 13.4 |
| 0.002 | 30.0 | 20.0 |
| 0.005 | 42.9 | 28.6 |
| 0.010 | 50.0 | 33.4 |
| 0.020 | 54.6 | 36.4 |
| 0.050 | 57.7 | 38.5 |
| 0.100 | 58.9 | 39.3 |
| 0.200 | 59.5 | 39.7 |
| 0.500 | 59.8 | 39.9 |
| 1.000 | 59.9 | 40.0 |
| 2.000 | 60.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect idio-competitive Incorrect inter-competitive Incorrect non-competitive Correct un-competitive Incorrect MC6a6a_dead
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 0.8 | 0.1 |
| 0.002 | 1.6 | 0.1 |
| 0.005 | 3.7 | 0.1 |
| 0.010 | 6.7 | 0.1 |
| 0.020 | 11.5 | 0.1 |
| 0.050 | 20.0 | 0.2 |
| 0.100 | 26.7 | 0.4 |
| 0.200 | 32.0 | 0.8 |
| 0.500 | 36.4 | 2.0 |
| 1.000 | 38.1 | 3.7 |
| 2.000 | 39.1 | 6.7 |
| 5.000 | 39.7 | 13.4 |
| 10.000 | 39.9 | 20.0 |
| 20.000 | 40.0 | 26.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
auto-competitive Incorrect competitive Correct non-competitive Incorrect poly-competitive Incorrect un-competitive Incorrect MC0cdc_26d3
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 20.0 | 20.0 |
| 0.002 | 30.0 | 26.7 |
| 0.005 | 42.9 | 33.4 |
| 0.010 | 50.0 | 36.4 |
| 0.020 | 54.6 | 38.1 |
| 0.050 | 57.7 | 39.3 |
| 0.100 | 58.9 | 39.7 |
| 0.200 | 59.5 | 39.9 |
| 0.500 | 59.8 | 40.0 |
| 1.000 | 59.9 | 40.0 |
| 2.000 | 60.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Incorrect para-competitive Incorrect pseudo-competitive Incorrect un-competitive Correct MC64dc_9f30
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 7.7 | 6.7 |
| 0.002 | 14.6 | 12.8 |
| 0.005 | 32.0 | 28.0 |
| 0.010 | 53.4 | 46.7 |
| 0.020 | 80.0 | 70.0 |
| 0.050 | 114.3 | 100.0 |
| 0.100 | 133.4 | 116.7 |
| 0.200 | 145.5 | 127.3 |
| 0.500 | 153.9 | 134.7 |
| 1.000 | 156.9 | 137.3 |
| 2.000 | 158.5 | 138.7 |
| 5.000 | 159.4 | 139.5 |
| 10.000 | 159.7 | 139.8 |
| 20.000 | 159.9 | 139.9 |
| 50.000 | 160.0 | 140.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect homo-competitive Incorrect non-competitive Correct oligo-competitive Incorrect un-competitive Incorrect MCe016_763c
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 2.0 | 1.0 |
| 0.002 | 3.7 | 1.9 |
| 0.005 | 8.0 | 4.0 |
| 0.010 | 13.4 | 6.7 |
| 0.020 | 20.0 | 10.0 |
| 0.050 | 28.6 | 14.3 |
| 0.100 | 33.4 | 16.7 |
| 0.200 | 36.4 | 18.2 |
| 0.500 | 38.5 | 19.3 |
| 1.000 | 39.3 | 19.7 |
| 2.000 | 39.7 | 19.9 |
| 5.000 | 39.9 | 20.0 |
| 10.000 | 40.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect idio-competitive Incorrect iso-competitive Incorrect non-competitive Correct un-competitive Incorrect MCca9b_834b
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 60.0 | 13.4 |
| 0.002 | 90.0 | 20.0 |
| 0.005 | 128.6 | 28.6 |
| 0.010 | 150.0 | 33.4 |
| 0.020 | 163.7 | 36.4 |
| 0.050 | 173.1 | 38.5 |
| 0.100 | 176.5 | 39.3 |
| 0.200 | 178.3 | 39.7 |
| 0.500 | 179.3 | 39.9 |
| 1.000 | 179.7 | 40.0 |
| 2.000 | 179.9 | 40.0 |
| 5.000 | 180.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect homo-competitive Incorrect non-competitive Correct semi-competitive Incorrect un-competitive Incorrect MC7b8a_a640
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 2.4 | 2.0 |
| 0.002 | 4.7 | 3.7 |
| 0.005 | 11.0 | 8.0 |
| 0.010 | 20.0 | 13.4 |
| 0.020 | 34.3 | 20.0 |
| 0.050 | 60.0 | 28.6 |
| 0.100 | 80.0 | 33.4 |
| 0.200 | 96.0 | 36.4 |
| 0.500 | 109.1 | 38.5 |
| 1.000 | 114.3 | 39.3 |
| 2.000 | 117.1 | 39.7 |
| 5.000 | 118.9 | 39.9 |
| 10.000 | 119.5 | 40.0 |
| 20.000 | 119.8 | 40.0 |
| 50.000 | 119.9 | 40.0 |
| 100.000 | 120.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
auto-competitive Incorrect competitive Incorrect non-competitive Incorrect post-competitive Incorrect un-competitive Correct MC3c10_9268
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 46.7 | 0.1 |
| 0.002 | 70.0 | 0.2 |
| 0.005 | 100.1 | 0.4 |
| 0.010 | 116.7 | 0.7 |
| 0.020 | 127.3 | 1.4 |
| 0.050 | 134.7 | 3.5 |
| 0.100 | 137.3 | 6.7 |
| 0.200 | 138.7 | 12.8 |
| 0.500 | 139.5 | 28.0 |
| 1.000 | 139.8 | 46.7 |
| 2.000 | 139.9 | 70.0 |
| 5.000 | 140.0 | 100.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct eco-competitive Incorrect non-competitive Incorrect proto-competitive Incorrect un-competitive Incorrect MC52b3_2094
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 5.8 | 2.4 |
| 0.002 | 11.0 | 4.7 |
| 0.005 | 24.0 | 11.0 |
| 0.010 | 40.0 | 20.0 |
| 0.020 | 60.0 | 34.3 |
| 0.050 | 85.8 | 60.0 |
| 0.100 | 100.0 | 80.0 |
| 0.200 | 109.1 | 96.0 |
| 0.500 | 115.4 | 109.1 |
| 1.000 | 117.7 | 114.3 |
| 2.000 | 118.9 | 117.1 |
| 5.000 | 119.6 | 118.9 |
| 10.000 | 119.8 | 119.5 |
| 20.000 | 119.9 | 119.8 |
| 50.000 | 120.0 | 119.9 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct non-competitive Incorrect ortho-competitive Incorrect pseudo-competitive Incorrect un-competitive Incorrect MCb8cb_1be0
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 6.7 | 4.8 |
| 0.002 | 12.8 | 9.1 |
| 0.005 | 28.0 | 20.0 |
| 0.010 | 46.7 | 33.4 |
| 0.020 | 70.0 | 50.0 |
| 0.050 | 100.0 | 71.5 |
| 0.100 | 116.7 | 83.4 |
| 0.200 | 127.3 | 91.0 |
| 0.500 | 134.7 | 96.2 |
| 1.000 | 137.3 | 98.1 |
| 2.000 | 138.7 | 99.1 |
| 5.000 | 139.5 | 99.7 |
| 10.000 | 139.8 | 99.9 |
| 20.000 | 139.9 | 100.0 |
| 50.000 | 140.0 | 100.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect intra-competitive Incorrect non-competitive Correct omni-competitive Incorrect un-competitive Incorrect MC6f4e_e1b1
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 26.7 | 13.4 |
| 0.002 | 45.8 | 22.9 |
| 0.005 | 80.0 | 40.0 |
| 0.010 | 106.7 | 53.4 |
| 0.020 | 128.0 | 64.0 |
| 0.050 | 145.5 | 72.8 |
| 0.100 | 152.4 | 76.2 |
| 0.200 | 156.1 | 78.1 |
| 0.500 | 158.5 | 79.3 |
| 1.000 | 159.3 | 79.7 |
| 2.000 | 159.7 | 79.9 |
| 5.000 | 159.9 | 80.0 |
| 10.000 | 160.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect iso-competitive Incorrect non-competitive Correct omni-competitive Incorrect un-competitive Incorrect MC3848_68e2
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 6.7 | 6.7 |
| 0.002 | 11.5 | 10.0 |
| 0.005 | 20.0 | 14.3 |
| 0.010 | 26.7 | 16.7 |
| 0.020 | 32.0 | 18.2 |
| 0.050 | 36.4 | 19.3 |
| 0.100 | 38.1 | 19.7 |
| 0.200 | 39.1 | 19.9 |
| 0.500 | 39.7 | 20.0 |
| 1.000 | 39.9 | 20.0 |
| 2.000 | 40.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect mis-competitive Incorrect non-competitive Incorrect poly-competitive Incorrect un-competitive Correct MC98dd_6cf7
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 5.5 | 0.1 |
| 0.002 | 10.0 | 0.1 |
| 0.005 | 20.0 | 0.1 |
| 0.010 | 30.0 | 0.1 |
| 0.020 | 40.0 | 0.2 |
| 0.050 | 50.0 | 0.3 |
| 0.100 | 54.6 | 0.6 |
| 0.200 | 57.2 | 1.2 |
| 0.500 | 58.9 | 2.9 |
| 1.000 | 59.5 | 5.5 |
| 2.000 | 59.8 | 10.0 |
| 5.000 | 59.9 | 20.0 |
| 10.000 | 60.0 | 30.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct inter-competitive Incorrect non-competitive Incorrect proto-competitive Incorrect un-competitive Incorrect MC9605_47e2
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 13.4 | 0.4 |
| 0.002 | 22.9 | 0.8 |
| 0.005 | 40.0 | 2.0 |
| 0.010 | 53.4 | 3.9 |
| 0.020 | 64.0 | 7.3 |
| 0.050 | 72.8 | 16.0 |
| 0.100 | 76.2 | 26.7 |
| 0.200 | 78.1 | 40.0 |
| 0.500 | 79.3 | 57.2 |
| 1.000 | 79.7 | 66.7 |
| 2.000 | 79.9 | 72.8 |
| 5.000 | 80.0 | 77.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct intra-competitive Incorrect non-competitive Incorrect oligo-competitive Incorrect un-competitive Incorrect MCba1d_1b30
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 30.0 | 0.1 |
| 0.002 | 51.5 | 0.1 |
| 0.005 | 90.0 | 0.2 |
| 0.010 | 120.1 | 0.4 |
| 0.020 | 144.0 | 0.8 |
| 0.050 | 163.7 | 1.8 |
| 0.100 | 171.5 | 3.6 |
| 0.200 | 175.7 | 7.0 |
| 0.500 | 178.3 | 16.4 |
| 1.000 | 179.2 | 30.0 |
| 2.000 | 179.6 | 51.5 |
| 5.000 | 179.9 | 90.0 |
| 10.000 | 180.0 | 120.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct hyper-competitive Incorrect non-competitive Incorrect pseudo-competitive Incorrect un-competitive Incorrect MC6762_6062
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 2.9 | 3.7 |
| 0.002 | 5.5 | 6.7 |
| 0.005 | 12.0 | 13.4 |
| 0.010 | 20.0 | 20.0 |
| 0.020 | 30.0 | 26.7 |
| 0.050 | 42.9 | 33.4 |
| 0.100 | 50.0 | 36.4 |
| 0.200 | 54.6 | 38.1 |
| 0.500 | 57.7 | 39.3 |
| 1.000 | 58.9 | 39.7 |
| 2.000 | 59.5 | 39.9 |
| 5.000 | 59.8 | 40.0 |
| 10.000 | 59.9 | 40.0 |
| 20.000 | 60.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect hyper-competitive Incorrect non-competitive Incorrect ortho-competitive Incorrect un-competitive Correct MCb292_16b9
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 16.7 | 6.7 |
| 0.002 | 28.6 | 11.5 |
| 0.005 | 50.0 | 20.0 |
| 0.010 | 66.7 | 26.7 |
| 0.020 | 80.0 | 32.0 |
| 0.050 | 91.0 | 36.4 |
| 0.100 | 95.3 | 38.1 |
| 0.200 | 97.6 | 39.1 |
| 0.500 | 99.1 | 39.7 |
| 1.000 | 99.6 | 39.9 |
| 2.000 | 99.8 | 40.0 |
| 5.000 | 100.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Correct super-competitive Incorrect supra-competitive Incorrect un-competitive Incorrect MC0ede_5a90
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 14.6 | 13.4 |
| 0.002 | 26.7 | 22.9 |
| 0.005 | 53.4 | 40.0 |
| 0.010 | 80.0 | 53.4 |
| 0.020 | 106.7 | 64.0 |
| 0.050 | 133.4 | 72.8 |
| 0.100 | 145.5 | 76.2 |
| 0.200 | 152.4 | 78.1 |
| 0.500 | 156.9 | 79.3 |
| 1.000 | 158.5 | 79.7 |
| 2.000 | 159.3 | 79.9 |
| 5.000 | 159.7 | 80.0 |
| 10.000 | 159.9 | 80.0 |
| 20.000 | 160.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect mis-competitive Incorrect non-competitive Incorrect oligo-competitive Incorrect un-competitive Correct MC2ac7_0f6a
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 53.4 | 40.0 |
| 0.002 | 80.0 | 60.0 |
| 0.005 | 114.3 | 85.8 |
| 0.010 | 133.4 | 100.0 |
| 0.020 | 145.5 | 109.1 |
| 0.050 | 153.9 | 115.4 |
| 0.100 | 156.9 | 117.7 |
| 0.200 | 158.5 | 118.9 |
| 0.500 | 159.4 | 119.6 |
| 1.000 | 159.7 | 119.8 |
| 2.000 | 159.9 | 119.9 |
| 5.000 | 160.0 | 120.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
anti-competitive Incorrect competitive Incorrect mega-competitive Incorrect non-competitive Correct un-competitive Incorrect MC414b_f84c
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 10.0 | 0.3 |
| 0.002 | 17.2 | 0.6 |
| 0.005 | 30.0 | 1.5 |
| 0.010 | 40.0 | 2.9 |
| 0.020 | 48.0 | 5.5 |
| 0.050 | 54.6 | 12.0 |
| 0.100 | 57.2 | 20.0 |
| 0.200 | 58.6 | 30.0 |
| 0.500 | 59.5 | 42.9 |
| 1.000 | 59.8 | 50.0 |
| 2.000 | 59.9 | 54.6 |
| 5.000 | 60.0 | 57.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct eco-competitive Incorrect non-competitive Incorrect over-competitive Incorrect un-competitive Incorrect MC6b7c_3f47
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 33.4 | 26.7 |
| 0.002 | 50.0 | 40.0 |
| 0.005 | 71.5 | 57.2 |
| 0.010 | 83.4 | 66.7 |
| 0.020 | 91.0 | 72.8 |
| 0.050 | 96.2 | 77.0 |
| 0.100 | 98.1 | 78.5 |
| 0.200 | 99.1 | 79.3 |
| 0.500 | 99.7 | 79.7 |
| 1.000 | 99.9 | 79.9 |
| 2.000 | 100.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Correct pre-competitive Incorrect semi-competitive Incorrect un-competitive Incorrect MC3bb0_11bc
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 23.4 | 12.8 |
| 0.002 | 40.0 | 23.4 |
| 0.005 | 70.0 | 46.7 |
| 0.010 | 93.4 | 70.0 |
| 0.020 | 112.0 | 93.4 |
| 0.050 | 127.3 | 116.7 |
| 0.100 | 133.4 | 127.3 |
| 0.200 | 136.6 | 133.4 |
| 0.500 | 138.7 | 137.3 |
| 1.000 | 139.4 | 138.7 |
| 2.000 | 139.7 | 139.4 |
| 5.000 | 139.9 | 139.8 |
| 10.000 | 140.0 | 139.9 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct non-competitive Incorrect para-competitive Incorrect super-competitive Incorrect un-competitive Incorrect MC7e0e_71c6
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 6.7 | 2.0 |
| 0.002 | 11.5 | 3.7 |
| 0.005 | 20.0 | 8.0 |
| 0.010 | 26.7 | 13.4 |
| 0.020 | 32.0 | 20.0 |
| 0.050 | 36.4 | 28.6 |
| 0.100 | 38.1 | 33.4 |
| 0.200 | 39.1 | 36.4 |
| 0.500 | 39.7 | 38.5 |
| 1.000 | 39.9 | 39.3 |
| 2.000 | 40.0 | 39.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct homo-competitive Incorrect iso-competitive Incorrect non-competitive Incorrect un-competitive Incorrect MCbb1d_b248
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 12.8 | 2.8 |
| 0.002 | 23.4 | 5.4 |
| 0.005 | 46.7 | 12.8 |
| 0.010 | 70.0 | 23.4 |
| 0.020 | 93.4 | 40.0 |
| 0.050 | 116.7 | 70.0 |
| 0.100 | 127.3 | 93.4 |
| 0.200 | 133.4 | 112.0 |
| 0.500 | 137.3 | 127.3 |
| 1.000 | 138.7 | 133.4 |
| 2.000 | 139.4 | 136.6 |
| 5.000 | 139.8 | 138.7 |
| 10.000 | 139.9 | 139.4 |
| 20.000 | 140.0 | 139.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct contra-competitive Incorrect iso-competitive Incorrect non-competitive Incorrect un-competitive Incorrect MC7459_f84c
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 10.0 | 3.4 |
| 0.002 | 17.2 | 5.8 |
| 0.005 | 30.0 | 10.0 |
| 0.010 | 40.0 | 13.4 |
| 0.020 | 48.0 | 16.0 |
| 0.050 | 54.6 | 18.2 |
| 0.100 | 57.2 | 19.1 |
| 0.200 | 58.6 | 19.6 |
| 0.500 | 59.5 | 19.9 |
| 1.000 | 59.8 | 20.0 |
| 2.000 | 59.9 | 20.0 |
| 5.000 | 60.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect eco-competitive Incorrect non-competitive Correct over-competitive Incorrect un-competitive Incorrect MCd250_fbb0
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 13.4 | 3.4 |
| 0.002 | 22.9 | 5.8 |
| 0.005 | 40.0 | 10.0 |
| 0.010 | 53.4 | 13.4 |
| 0.020 | 64.0 | 16.0 |
| 0.050 | 72.8 | 18.2 |
| 0.100 | 76.2 | 19.1 |
| 0.200 | 78.1 | 19.6 |
| 0.500 | 79.3 | 19.9 |
| 1.000 | 79.7 | 20.0 |
| 2.000 | 79.9 | 20.0 |
| 5.000 | 80.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Correct pseudo-competitive Incorrect quasi-competitive Incorrect un-competitive Incorrect MC680e_1be0
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 5.8 | 1.0 |
| 0.002 | 11.0 | 1.9 |
| 0.005 | 24.0 | 4.0 |
| 0.010 | 40.0 | 6.7 |
| 0.020 | 60.0 | 10.0 |
| 0.050 | 85.8 | 14.3 |
| 0.100 | 100.0 | 16.7 |
| 0.200 | 109.1 | 18.2 |
| 0.500 | 115.4 | 19.3 |
| 1.000 | 117.7 | 19.7 |
| 2.000 | 118.9 | 19.9 |
| 5.000 | 119.6 | 20.0 |
| 10.000 | 119.8 | 20.0 |
| 20.000 | 119.9 | 20.0 |
| 50.000 | 120.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect intra-competitive Incorrect non-competitive Correct omni-competitive Incorrect un-competitive Incorrect MC869c_6849
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 3.2 | 1.2 |
| 0.002 | 6.2 | 2.4 |
| 0.005 | 14.6 | 5.5 |
| 0.010 | 26.7 | 10.0 |
| 0.020 | 45.8 | 17.2 |
| 0.050 | 80.0 | 30.0 |
| 0.100 | 106.7 | 40.0 |
| 0.200 | 128.0 | 48.0 |
| 0.500 | 145.5 | 54.6 |
| 1.000 | 152.4 | 57.2 |
| 2.000 | 156.1 | 58.6 |
| 5.000 | 158.5 | 59.5 |
| 10.000 | 159.3 | 59.8 |
| 20.000 | 159.7 | 59.9 |
| 50.000 | 159.9 | 60.0 |
| 100.000 | 160.0 | 60.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Correct ortho-competitive Incorrect poly-competitive Incorrect un-competitive Incorrect MCa909_1be0
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 6.7 | 2.8 |
| 0.002 | 12.8 | 5.4 |
| 0.005 | 28.0 | 12.8 |
| 0.010 | 46.7 | 23.4 |
| 0.020 | 70.0 | 40.0 |
| 0.050 | 100.0 | 70.0 |
| 0.100 | 116.7 | 93.4 |
| 0.200 | 127.3 | 112.0 |
| 0.500 | 134.7 | 127.3 |
| 1.000 | 137.3 | 133.4 |
| 2.000 | 138.7 | 136.6 |
| 5.000 | 139.5 | 138.7 |
| 10.000 | 139.8 | 139.4 |
| 20.000 | 139.9 | 139.7 |
| 50.000 | 140.0 | 139.9 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct intra-competitive Incorrect non-competitive Incorrect omni-competitive Incorrect un-competitive Incorrect MCb710_5d52
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 2.0 | 0.1 |
| 0.002 | 3.7 | 0.1 |
| 0.005 | 8.0 | 0.1 |
| 0.010 | 13.4 | 0.1 |
| 0.020 | 20.0 | 0.2 |
| 0.050 | 28.6 | 0.4 |
| 0.100 | 33.4 | 0.8 |
| 0.200 | 36.4 | 1.6 |
| 0.500 | 38.5 | 3.7 |
| 1.000 | 39.3 | 6.7 |
| 2.000 | 39.7 | 11.5 |
| 5.000 | 39.9 | 20.0 |
| 10.000 | 40.0 | 26.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
anti-competitive Incorrect competitive Correct non-competitive Incorrect pre-competitive Incorrect un-competitive Incorrect MC28aa_9c5d
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 12.8 | 9.1 |
| 0.002 | 23.4 | 16.7 |
| 0.005 | 46.7 | 33.4 |
| 0.010 | 70.0 | 50.0 |
| 0.020 | 93.4 | 66.7 |
| 0.050 | 116.7 | 83.4 |
| 0.100 | 127.3 | 91.0 |
| 0.200 | 133.4 | 95.3 |
| 0.500 | 137.3 | 98.1 |
| 1.000 | 138.7 | 99.1 |
| 2.000 | 139.4 | 99.6 |
| 5.000 | 139.8 | 99.9 |
| 10.000 | 139.9 | 100.0 |
| 20.000 | 140.0 | 100.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect epi-competitive Incorrect hetero-competitive Incorrect non-competitive Correct un-competitive Incorrect MCdc24_9645
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 8.6 | 0.1 |
| 0.002 | 16.4 | 0.1 |
| 0.005 | 36.0 | 0.2 |
| 0.010 | 60.1 | 0.4 |
| 0.020 | 90.0 | 0.8 |
| 0.050 | 128.6 | 1.8 |
| 0.100 | 150.0 | 3.6 |
| 0.200 | 163.7 | 7.0 |
| 0.500 | 173.1 | 16.4 |
| 1.000 | 176.5 | 30.0 |
| 2.000 | 178.3 | 51.5 |
| 5.000 | 179.3 | 90.0 |
| 10.000 | 179.7 | 120.0 |
| 20.000 | 179.9 | 144.0 |
| 50.000 | 180.0 | 163.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct non-competitive Incorrect post-competitive Incorrect ultra-competitive Incorrect un-competitive Incorrect MCd1f1_e80f
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 2.4 | 0.2 |
| 0.002 | 4.7 | 0.3 |
| 0.005 | 11.0 | 0.6 |
| 0.010 | 20.0 | 1.2 |
| 0.020 | 34.3 | 2.4 |
| 0.050 | 60.0 | 5.8 |
| 0.100 | 80.0 | 11.0 |
| 0.200 | 96.0 | 20.0 |
| 0.500 | 109.1 | 40.0 |
| 1.000 | 114.3 | 60.0 |
| 2.000 | 117.1 | 80.0 |
| 5.000 | 118.9 | 100.0 |
| 10.000 | 119.5 | 109.1 |
| 20.000 | 119.8 | 114.3 |
| 50.000 | 119.9 | 117.7 |
| 100.000 | 120.0 | 118.9 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct contra-competitive Incorrect hetero-competitive Incorrect non-competitive Incorrect un-competitive Incorrect MC38cc_9fc3
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 16.4 | 13.4 |
| 0.002 | 30.0 | 22.9 |
| 0.005 | 60.1 | 40.0 |
| 0.010 | 90.0 | 53.4 |
| 0.020 | 120.1 | 64.0 |
| 0.050 | 150.0 | 72.8 |
| 0.100 | 163.7 | 76.2 |
| 0.200 | 171.5 | 78.1 |
| 0.500 | 176.5 | 79.3 |
| 1.000 | 178.3 | 79.7 |
| 2.000 | 179.2 | 79.9 |
| 5.000 | 179.7 | 80.0 |
| 10.000 | 179.9 | 80.0 |
| 20.000 | 180.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
auto-competitive Incorrect competitive Incorrect non-competitive Incorrect super-competitive Incorrect un-competitive Correct MC0014_5fec
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 4.0 | 3.9 |
| 0.002 | 7.7 | 7.3 |
| 0.005 | 18.2 | 16.0 |
| 0.010 | 33.4 | 26.7 |
| 0.020 | 57.2 | 40.0 |
| 0.050 | 100.0 | 57.2 |
| 0.100 | 133.4 | 66.7 |
| 0.200 | 160.0 | 72.8 |
| 0.500 | 181.9 | 77.0 |
| 1.000 | 190.5 | 78.5 |
| 2.000 | 195.2 | 79.3 |
| 5.000 | 198.1 | 79.7 |
| 10.000 | 199.1 | 79.9 |
| 20.000 | 199.6 | 80.0 |
| 50.000 | 199.9 | 80.0 |
| 100.000 | 200.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Incorrect pre-competitive Incorrect quasi-competitive Incorrect un-competitive Correct MC81d6_4aa9
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 40.0 | 0.1 |
| 0.002 | 60.0 | 0.2 |
| 0.005 | 85.8 | 0.3 |
| 0.010 | 100.0 | 0.6 |
| 0.020 | 109.1 | 1.2 |
| 0.050 | 115.4 | 3.0 |
| 0.100 | 117.7 | 5.8 |
| 0.200 | 118.9 | 11.0 |
| 0.500 | 119.6 | 24.0 |
| 1.000 | 119.8 | 40.0 |
| 2.000 | 119.9 | 60.0 |
| 5.000 | 120.0 | 85.8 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct contra-competitive Incorrect dis-competitive Incorrect non-competitive Incorrect un-competitive Incorrect MC594c_9268
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 3.7 | 3.4 |
| 0.002 | 6.7 | 5.8 |
| 0.005 | 13.4 | 10.0 |
| 0.010 | 20.0 | 13.4 |
| 0.020 | 26.7 | 16.0 |
| 0.050 | 33.4 | 18.2 |
| 0.100 | 36.4 | 19.1 |
| 0.200 | 38.1 | 19.6 |
| 0.500 | 39.3 | 19.9 |
| 1.000 | 39.7 | 20.0 |
| 2.000 | 39.9 | 20.0 |
| 5.000 | 40.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect eco-competitive Incorrect non-competitive Incorrect proto-competitive Incorrect un-competitive Correct MC4ba7_20ca
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 16.4 | 5.5 |
| 0.002 | 30.0 | 10.0 |
| 0.005 | 60.1 | 20.0 |
| 0.010 | 90.0 | 30.0 |
| 0.020 | 120.1 | 40.0 |
| 0.050 | 150.0 | 50.0 |
| 0.100 | 163.7 | 54.6 |
| 0.200 | 171.5 | 57.2 |
| 0.500 | 176.5 | 58.9 |
| 1.000 | 178.3 | 59.5 |
| 2.000 | 179.2 | 59.8 |
| 5.000 | 179.7 | 59.9 |
| 10.000 | 179.9 | 60.0 |
| 20.000 | 180.0 | 60.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect contra-competitive Incorrect intra-competitive Incorrect non-competitive Correct un-competitive Incorrect MCc313_a20d
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 3.7 | 0.1 |
| 0.002 | 6.7 | 0.1 |
| 0.005 | 13.4 | 0.2 |
| 0.010 | 20.0 | 0.4 |
| 0.020 | 26.7 | 0.8 |
| 0.050 | 33.4 | 2.0 |
| 0.100 | 36.4 | 3.7 |
| 0.200 | 38.1 | 6.7 |
| 0.500 | 39.3 | 13.4 |
| 1.000 | 39.7 | 20.0 |
| 2.000 | 39.9 | 26.7 |
| 5.000 | 40.0 | 33.4 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct dis-competitive Incorrect non-competitive Incorrect over-competitive Incorrect un-competitive Incorrect MC08ae_0a92
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 1.6 | 2.0 |
| 0.002 | 3.1 | 3.7 |
| 0.005 | 7.3 | 8.0 |
| 0.010 | 13.4 | 13.4 |
| 0.020 | 22.9 | 20.0 |
| 0.050 | 40.0 | 28.6 |
| 0.100 | 53.4 | 33.4 |
| 0.200 | 64.0 | 36.4 |
| 0.500 | 72.8 | 38.5 |
| 1.000 | 76.2 | 39.3 |
| 2.000 | 78.1 | 39.7 |
| 5.000 | 79.3 | 39.9 |
| 10.000 | 79.7 | 40.0 |
| 20.000 | 79.9 | 40.0 |
| 50.000 | 80.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect hetero-competitive Incorrect non-competitive Incorrect oligo-competitive Incorrect un-competitive Correct MCf162_adc6
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 5.8 | 5.5 |
| 0.002 | 11.0 | 10.0 |
| 0.005 | 24.0 | 20.0 |
| 0.010 | 40.0 | 30.0 |
| 0.020 | 60.0 | 40.0 |
| 0.050 | 85.8 | 50.0 |
| 0.100 | 100.0 | 54.6 |
| 0.200 | 109.1 | 57.2 |
| 0.500 | 115.4 | 58.9 |
| 1.000 | 117.7 | 59.5 |
| 2.000 | 118.9 | 59.8 |
| 5.000 | 119.6 | 59.9 |
| 10.000 | 119.8 | 60.0 |
| 20.000 | 119.9 | 60.0 |
| 50.000 | 120.0 | 60.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Incorrect over-competitive Incorrect super-competitive Incorrect un-competitive Correct MCa447_5bda
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 3.9 | 3.7 |
| 0.002 | 7.3 | 6.7 |
| 0.005 | 16.0 | 13.4 |
| 0.010 | 26.7 | 20.0 |
| 0.020 | 40.0 | 26.7 |
| 0.050 | 57.2 | 33.4 |
| 0.100 | 66.7 | 36.4 |
| 0.200 | 72.8 | 38.1 |
| 0.500 | 77.0 | 39.3 |
| 1.000 | 78.5 | 39.7 |
| 2.000 | 79.3 | 39.9 |
| 5.000 | 79.7 | 40.0 |
| 10.000 | 79.9 | 40.0 |
| 20.000 | 80.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect dis-competitive Incorrect non-competitive Incorrect super-competitive Incorrect un-competitive Correct MCd1ab_e165
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 3.9 | 1.0 |
| 0.002 | 7.3 | 1.9 |
| 0.005 | 16.0 | 4.0 |
| 0.010 | 26.7 | 6.7 |
| 0.020 | 40.0 | 10.0 |
| 0.050 | 57.2 | 14.3 |
| 0.100 | 66.7 | 16.7 |
| 0.200 | 72.8 | 18.2 |
| 0.500 | 77.0 | 19.3 |
| 1.000 | 78.5 | 19.7 |
| 2.000 | 79.3 | 19.9 |
| 5.000 | 79.7 | 20.0 |
| 10.000 | 79.9 | 20.0 |
| 20.000 | 80.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect eco-competitive Incorrect non-competitive Correct super-competitive Incorrect un-competitive Incorrect MCccad_a45e
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 26.7 | 0.1 |
| 0.002 | 45.8 | 0.1 |
| 0.005 | 80.0 | 0.1 |
| 0.010 | 106.7 | 0.2 |
| 0.020 | 128.0 | 0.4 |
| 0.050 | 145.5 | 0.8 |
| 0.100 | 152.4 | 1.6 |
| 0.200 | 156.1 | 3.2 |
| 0.500 | 158.5 | 7.7 |
| 1.000 | 159.3 | 14.6 |
| 2.000 | 159.7 | 26.7 |
| 5.000 | 159.9 | 53.4 |
| 10.000 | 160.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
auto-competitive Incorrect competitive Correct non-competitive Incorrect self-competitive Incorrect un-competitive Incorrect MCa87a_e2f0
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 2.0 | 2.0 |
| 0.002 | 3.9 | 3.7 |
| 0.005 | 9.1 | 8.0 |
| 0.010 | 16.7 | 13.4 |
| 0.020 | 28.6 | 20.0 |
| 0.050 | 50.0 | 28.6 |
| 0.100 | 66.7 | 33.4 |
| 0.200 | 80.0 | 36.4 |
| 0.500 | 91.0 | 38.5 |
| 1.000 | 95.3 | 39.3 |
| 2.000 | 97.6 | 39.7 |
| 5.000 | 99.1 | 39.9 |
| 10.000 | 99.6 | 40.0 |
| 20.000 | 99.8 | 40.0 |
| 50.000 | 100.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect iso-competitive Incorrect non-competitive Incorrect semi-competitive Incorrect un-competitive Correct MC23c1_d1e8
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 20.0 | 3.4 |
| 0.002 | 34.3 | 5.8 |
| 0.005 | 60.0 | 10.0 |
| 0.010 | 80.0 | 13.4 |
| 0.020 | 96.0 | 16.0 |
| 0.050 | 109.1 | 18.2 |
| 0.100 | 114.3 | 19.1 |
| 0.200 | 117.1 | 19.6 |
| 0.500 | 118.9 | 19.9 |
| 1.000 | 119.5 | 20.0 |
| 2.000 | 119.8 | 20.0 |
| 5.000 | 119.9 | 20.0 |
| 10.000 | 120.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect intra-competitive Incorrect iso-competitive Incorrect non-competitive Correct un-competitive Incorrect MC79d9_c242
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 0.8 | 0.4 |
| 0.002 | 1.6 | 0.8 |
| 0.005 | 3.7 | 1.9 |
| 0.010 | 6.7 | 3.4 |
| 0.020 | 11.5 | 5.8 |
| 0.050 | 20.0 | 10.0 |
| 0.100 | 26.7 | 13.4 |
| 0.200 | 32.0 | 16.0 |
| 0.500 | 36.4 | 18.2 |
| 1.000 | 38.1 | 19.1 |
| 2.000 | 39.1 | 19.6 |
| 5.000 | 39.7 | 19.9 |
| 10.000 | 39.9 | 20.0 |
| 20.000 | 40.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect mega-competitive Incorrect non-competitive Correct ortho-competitive Incorrect un-competitive Incorrect MCdd03_b1e8
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 33.4 | 23.4 |
| 0.002 | 57.2 | 40.0 |
| 0.005 | 100.0 | 70.0 |
| 0.010 | 133.4 | 93.4 |
| 0.020 | 160.0 | 112.0 |
| 0.050 | 181.9 | 127.3 |
| 0.100 | 190.5 | 133.4 |
| 0.200 | 195.2 | 136.6 |
| 0.500 | 198.1 | 138.7 |
| 1.000 | 199.1 | 139.4 |
| 2.000 | 199.6 | 139.7 |
| 5.000 | 199.9 | 139.9 |
| 10.000 | 200.0 | 140.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Correct pre-competitive Incorrect supra-competitive Incorrect un-competitive Incorrect MCa1ce_3227
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 7.3 | 1.9 |
| 0.002 | 13.4 | 3.4 |
| 0.005 | 26.7 | 6.7 |
| 0.010 | 40.0 | 10.0 |
| 0.020 | 53.4 | 13.4 |
| 0.050 | 66.7 | 16.7 |
| 0.100 | 72.8 | 18.2 |
| 0.200 | 76.2 | 19.1 |
| 0.500 | 78.5 | 19.7 |
| 1.000 | 79.3 | 19.9 |
| 2.000 | 79.7 | 20.0 |
| 5.000 | 79.9 | 20.0 |
| 10.000 | 80.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect idio-competitive Incorrect non-competitive Correct self-competitive Incorrect un-competitive Incorrect MC2f3e_d875
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 1.2 | 0.3 |
| 0.002 | 2.4 | 0.6 |
| 0.005 | 5.5 | 1.5 |
| 0.010 | 10.0 | 2.9 |
| 0.020 | 17.2 | 5.5 |
| 0.050 | 30.0 | 12.0 |
| 0.100 | 40.0 | 20.0 |
| 0.200 | 48.0 | 30.0 |
| 0.500 | 54.6 | 42.9 |
| 1.000 | 57.2 | 50.0 |
| 2.000 | 58.6 | 54.6 |
| 5.000 | 59.5 | 57.7 |
| 10.000 | 59.8 | 58.9 |
| 20.000 | 59.9 | 59.5 |
| 50.000 | 60.0 | 59.8 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
anti-competitive Incorrect competitive Correct non-competitive Incorrect poly-competitive Incorrect un-competitive Incorrect MC3386_73b9
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 7.7 | 3.2 |
| 0.002 | 14.6 | 6.2 |
| 0.005 | 32.0 | 14.6 |
| 0.010 | 53.4 | 26.7 |
| 0.020 | 80.0 | 45.8 |
| 0.050 | 114.3 | 80.0 |
| 0.100 | 133.4 | 106.7 |
| 0.200 | 145.5 | 128.0 |
| 0.500 | 153.9 | 145.5 |
| 1.000 | 156.9 | 152.4 |
| 2.000 | 158.5 | 156.1 |
| 5.000 | 159.4 | 158.5 |
| 10.000 | 159.7 | 159.3 |
| 20.000 | 159.9 | 159.7 |
| 50.000 | 160.0 | 159.9 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct non-competitive Incorrect omni-competitive Incorrect super-competitive Incorrect un-competitive Incorrect MC793b_074d
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 7.3 | 6.7 |
| 0.002 | 13.4 | 11.5 |
| 0.005 | 26.7 | 20.0 |
| 0.010 | 40.0 | 26.7 |
| 0.020 | 53.4 | 32.0 |
| 0.050 | 66.7 | 36.4 |
| 0.100 | 72.8 | 38.1 |
| 0.200 | 76.2 | 39.1 |
| 0.500 | 78.5 | 39.7 |
| 1.000 | 79.3 | 39.9 |
| 2.000 | 79.7 | 40.0 |
| 5.000 | 79.9 | 40.0 |
| 10.000 | 80.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
anti-competitive Incorrect competitive Incorrect dis-competitive Incorrect non-competitive Incorrect un-competitive Correct MCdba0_c455
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 33.4 | 4.0 |
| 0.002 | 57.2 | 7.7 |
| 0.005 | 100.0 | 18.2 |
| 0.010 | 133.4 | 33.4 |
| 0.020 | 160.0 | 57.2 |
| 0.050 | 181.9 | 100.0 |
| 0.100 | 190.5 | 133.4 |
| 0.200 | 195.2 | 160.0 |
| 0.500 | 198.1 | 181.9 |
| 1.000 | 199.1 | 190.5 |
| 2.000 | 199.6 | 195.2 |
| 5.000 | 199.9 | 198.1 |
| 10.000 | 200.0 | 199.1 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct non-competitive Incorrect poly-competitive Incorrect supra-competitive Incorrect un-competitive Incorrect MCb06d_1593
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 33.4 | 2.0 |
| 0.002 | 50.0 | 3.9 |
| 0.005 | 71.5 | 9.1 |
| 0.010 | 83.4 | 16.7 |
| 0.020 | 91.0 | 28.6 |
| 0.050 | 96.2 | 50.0 |
| 0.100 | 98.1 | 66.7 |
| 0.200 | 99.1 | 80.0 |
| 0.500 | 99.7 | 91.0 |
| 1.000 | 99.9 | 95.3 |
| 2.000 | 100.0 | 97.6 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct hypo-competitive Incorrect non-competitive Incorrect ortho-competitive Incorrect un-competitive Incorrect MCf32e_b8b1
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 60.0 | 40.0 |
| 0.002 | 90.0 | 53.4 |
| 0.005 | 128.6 | 66.7 |
| 0.010 | 150.0 | 72.8 |
| 0.020 | 163.7 | 76.2 |
| 0.050 | 173.1 | 78.5 |
| 0.100 | 176.5 | 79.3 |
| 0.200 | 178.3 | 79.7 |
| 0.500 | 179.3 | 79.9 |
| 1.000 | 179.7 | 80.0 |
| 2.000 | 179.9 | 80.0 |
| 5.000 | 180.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
anti-competitive Incorrect competitive Incorrect hyper-competitive Incorrect non-competitive Incorrect un-competitive Correct MC12c3_7497
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 4.0 | 0.4 |
| 0.002 | 7.7 | 0.8 |
| 0.005 | 18.2 | 1.9 |
| 0.010 | 33.4 | 3.4 |
| 0.020 | 57.2 | 5.8 |
| 0.050 | 100.0 | 10.0 |
| 0.100 | 133.4 | 13.4 |
| 0.200 | 160.0 | 16.0 |
| 0.500 | 181.9 | 18.2 |
| 1.000 | 190.5 | 19.1 |
| 2.000 | 195.2 | 19.6 |
| 5.000 | 198.1 | 19.9 |
| 10.000 | 199.1 | 20.0 |
| 20.000 | 199.6 | 20.0 |
| 50.000 | 199.9 | 20.0 |
| 100.000 | 200.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect iso-competitive Incorrect mega-competitive Incorrect non-competitive Correct un-competitive Incorrect MCf60f_9232
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 18.2 | 14.6 |
| 0.002 | 33.4 | 26.7 |
| 0.005 | 66.7 | 53.4 |
| 0.010 | 100.0 | 80.0 |
| 0.020 | 133.4 | 106.7 |
| 0.050 | 166.7 | 133.4 |
| 0.100 | 181.9 | 145.5 |
| 0.200 | 190.5 | 152.4 |
| 0.500 | 196.1 | 156.9 |
| 1.000 | 198.1 | 158.5 |
| 2.000 | 199.1 | 159.3 |
| 5.000 | 199.7 | 159.7 |
| 10.000 | 199.9 | 159.9 |
| 20.000 | 200.0 | 160.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect contra-competitive Incorrect non-competitive Correct proto-competitive Incorrect un-competitive Incorrect MCcfaf_0f3a
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 13.4 | 6.7 |
| 0.002 | 20.0 | 10.0 |
| 0.005 | 28.6 | 14.3 |
| 0.010 | 33.4 | 16.7 |
| 0.020 | 36.4 | 18.2 |
| 0.050 | 38.5 | 19.3 |
| 0.100 | 39.3 | 19.7 |
| 0.200 | 39.7 | 19.9 |
| 0.500 | 39.9 | 20.0 |
| 1.000 | 40.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect eco-competitive Incorrect extra-competitive Incorrect non-competitive Correct un-competitive Incorrect MCfa93_59d9
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 26.7 | 20.0 |
| 0.002 | 40.0 | 30.0 |
| 0.005 | 57.2 | 42.9 |
| 0.010 | 66.7 | 50.0 |
| 0.020 | 72.8 | 54.6 |
| 0.050 | 77.0 | 57.7 |
| 0.100 | 78.5 | 58.9 |
| 0.200 | 79.3 | 59.5 |
| 0.500 | 79.7 | 59.8 |
| 1.000 | 79.9 | 59.9 |
| 2.000 | 80.0 | 60.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect intra-competitive Incorrect non-competitive Correct poly-competitive Incorrect un-competitive Incorrect MCe735_30a3
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 2.9 | 0.1 |
| 0.002 | 5.5 | 0.1 |
| 0.005 | 12.0 | 0.1 |
| 0.010 | 20.0 | 0.1 |
| 0.020 | 30.0 | 0.2 |
| 0.050 | 42.9 | 0.3 |
| 0.100 | 50.0 | 0.6 |
| 0.200 | 54.6 | 1.2 |
| 0.500 | 57.7 | 2.9 |
| 1.000 | 58.9 | 5.5 |
| 2.000 | 59.5 | 10.0 |
| 5.000 | 59.8 | 20.0 |
| 10.000 | 59.9 | 30.0 |
| 20.000 | 60.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct non-competitive Incorrect over-competitive Incorrect semi-competitive Incorrect un-competitive Incorrect MCc51d_0c7d
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 66.7 | 60.0 |
| 0.002 | 100.0 | 90.0 |
| 0.005 | 142.9 | 128.6 |
| 0.010 | 166.7 | 150.0 |
| 0.020 | 181.9 | 163.7 |
| 0.050 | 192.4 | 173.1 |
| 0.100 | 196.1 | 176.5 |
| 0.200 | 198.1 | 178.3 |
| 0.500 | 199.3 | 179.3 |
| 1.000 | 199.7 | 179.7 |
| 2.000 | 199.9 | 179.9 |
| 5.000 | 200.0 | 180.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect idio-competitive Incorrect non-competitive Correct supra-competitive Incorrect un-competitive Incorrect MCe795_2296
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 4.8 | 0.1 |
| 0.002 | 9.1 | 0.1 |
| 0.005 | 20.0 | 0.1 |
| 0.010 | 33.4 | 0.1 |
| 0.020 | 50.0 | 0.2 |
| 0.050 | 71.5 | 0.5 |
| 0.100 | 83.4 | 1.0 |
| 0.200 | 91.0 | 2.0 |
| 0.500 | 96.2 | 4.8 |
| 1.000 | 98.1 | 9.1 |
| 2.000 | 99.1 | 16.7 |
| 5.000 | 99.7 | 33.4 |
| 10.000 | 99.9 | 50.0 |
| 20.000 | 100.0 | 66.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct extra-competitive Incorrect homo-competitive Incorrect non-competitive Incorrect un-competitive Incorrect MC9268_bf1d
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 5.5 | 6.7 |
| 0.002 | 10.0 | 11.5 |
| 0.005 | 20.0 | 20.0 |
| 0.010 | 30.0 | 26.7 |
| 0.020 | 40.0 | 32.0 |
| 0.050 | 50.0 | 36.4 |
| 0.100 | 54.6 | 38.1 |
| 0.200 | 57.2 | 39.1 |
| 0.500 | 58.9 | 39.7 |
| 1.000 | 59.5 | 39.9 |
| 2.000 | 59.8 | 40.0 |
| 5.000 | 59.9 | 40.0 |
| 10.000 | 60.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Incorrect oligo-competitive Incorrect over-competitive Incorrect un-competitive Correct MC466d_00b4
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 9.6 | 2.9 |
| 0.002 | 18.2 | 5.5 |
| 0.005 | 40.0 | 12.0 |
| 0.010 | 66.7 | 20.0 |
| 0.020 | 100.0 | 30.0 |
| 0.050 | 142.9 | 42.9 |
| 0.100 | 166.7 | 50.0 |
| 0.200 | 181.9 | 54.6 |
| 0.500 | 192.4 | 57.7 |
| 1.000 | 196.1 | 58.9 |
| 2.000 | 198.1 | 59.5 |
| 5.000 | 199.3 | 59.8 |
| 10.000 | 199.7 | 59.9 |
| 20.000 | 199.9 | 60.0 |
| 50.000 | 200.0 | 60.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Correct omni-competitive Incorrect proto-competitive Incorrect un-competitive Incorrect MC0849_de0f
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 2.8 | 2.9 |
| 0.002 | 5.4 | 5.5 |
| 0.005 | 12.8 | 12.0 |
| 0.010 | 23.4 | 20.0 |
| 0.020 | 40.0 | 30.0 |
| 0.050 | 70.0 | 42.9 |
| 0.100 | 93.4 | 50.0 |
| 0.200 | 112.0 | 54.6 |
| 0.500 | 127.3 | 57.7 |
| 1.000 | 133.4 | 58.9 |
| 2.000 | 136.6 | 59.5 |
| 5.000 | 138.7 | 59.8 |
| 10.000 | 139.4 | 59.9 |
| 20.000 | 139.7 | 60.0 |
| 50.000 | 139.9 | 60.0 |
| 100.000 | 140.0 | 60.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect inter-competitive Incorrect intra-competitive Incorrect non-competitive Incorrect un-competitive Correct MC8a44_3233
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 2.8 | 1.6 |
| 0.002 | 5.4 | 3.1 |
| 0.005 | 12.8 | 7.3 |
| 0.010 | 23.4 | 13.4 |
| 0.020 | 40.0 | 22.9 |
| 0.050 | 70.0 | 40.0 |
| 0.100 | 93.4 | 53.4 |
| 0.200 | 112.0 | 64.0 |
| 0.500 | 127.3 | 72.8 |
| 1.000 | 133.4 | 76.2 |
| 2.000 | 136.6 | 78.1 |
| 5.000 | 138.7 | 79.3 |
| 10.000 | 139.4 | 79.7 |
| 20.000 | 139.7 | 79.9 |
| 50.000 | 139.9 | 80.0 |
| 100.000 | 140.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Correct para-competitive Incorrect self-competitive Incorrect un-competitive Incorrect MCea46_4d7c
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 6.7 | 3.4 |
| 0.002 | 11.5 | 5.8 |
| 0.005 | 20.0 | 10.0 |
| 0.010 | 26.7 | 13.4 |
| 0.020 | 32.0 | 16.0 |
| 0.050 | 36.4 | 18.2 |
| 0.100 | 38.1 | 19.1 |
| 0.200 | 39.1 | 19.6 |
| 0.500 | 39.7 | 19.9 |
| 1.000 | 39.9 | 20.0 |
| 2.000 | 40.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect extra-competitive Incorrect iso-competitive Incorrect non-competitive Correct un-competitive Incorrect MC174d_7497
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 30.0 | 23.4 |
| 0.002 | 51.5 | 40.0 |
| 0.005 | 90.0 | 70.0 |
| 0.010 | 120.1 | 93.4 |
| 0.020 | 144.0 | 112.0 |
| 0.050 | 163.7 | 127.3 |
| 0.100 | 171.5 | 133.4 |
| 0.200 | 175.7 | 136.6 |
| 0.500 | 178.3 | 138.7 |
| 1.000 | 179.2 | 139.4 |
| 2.000 | 179.6 | 139.7 |
| 5.000 | 179.9 | 139.9 |
| 10.000 | 180.0 | 140.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect iso-competitive Incorrect mega-competitive Incorrect non-competitive Correct un-competitive Incorrect MC7399_2027
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 11.0 | 2.4 |
| 0.002 | 20.0 | 4.7 |
| 0.005 | 40.0 | 11.0 |
| 0.010 | 60.0 | 20.0 |
| 0.020 | 80.0 | 34.3 |
| 0.050 | 100.0 | 60.0 |
| 0.100 | 109.1 | 80.0 |
| 0.200 | 114.3 | 96.0 |
| 0.500 | 117.7 | 109.1 |
| 1.000 | 118.9 | 114.3 |
| 2.000 | 119.5 | 117.1 |
| 5.000 | 119.8 | 118.9 |
| 10.000 | 119.9 | 119.5 |
| 20.000 | 120.0 | 119.8 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct non-competitive Incorrect proto-competitive Incorrect self-competitive Incorrect un-competitive Incorrect MCa125_f985
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 1.6 | 0.1 |
| 0.002 | 3.1 | 0.1 |
| 0.005 | 7.3 | 0.2 |
| 0.010 | 13.4 | 0.4 |
| 0.020 | 22.9 | 0.8 |
| 0.050 | 40.0 | 2.0 |
| 0.100 | 53.4 | 3.9 |
| 0.200 | 64.0 | 7.3 |
| 0.500 | 72.8 | 16.0 |
| 1.000 | 76.2 | 26.7 |
| 2.000 | 78.1 | 40.0 |
| 5.000 | 79.3 | 57.2 |
| 10.000 | 79.7 | 66.7 |
| 20.000 | 79.9 | 72.8 |
| 50.000 | 80.0 | 77.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct hetero-competitive Incorrect mega-competitive Incorrect non-competitive Incorrect un-competitive Incorrect MC8399_f53d
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 9.6 | 9.1 |
| 0.002 | 18.2 | 16.7 |
| 0.005 | 40.0 | 33.4 |
| 0.010 | 66.7 | 50.0 |
| 0.020 | 100.0 | 66.7 |
| 0.050 | 142.9 | 83.4 |
| 0.100 | 166.7 | 91.0 |
| 0.200 | 181.9 | 95.3 |
| 0.500 | 192.4 | 98.1 |
| 1.000 | 196.1 | 99.1 |
| 2.000 | 198.1 | 99.6 |
| 5.000 | 199.3 | 99.9 |
| 10.000 | 199.7 | 100.0 |
| 20.000 | 199.9 | 100.0 |
| 50.000 | 200.0 | 100.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect contra-competitive Incorrect mis-competitive Incorrect non-competitive Incorrect un-competitive Correct MCea20_13c5
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 1.2 | 1.0 |
| 0.002 | 2.4 | 1.9 |
| 0.005 | 5.5 | 4.0 |
| 0.010 | 10.0 | 6.7 |
| 0.020 | 17.2 | 10.0 |
| 0.050 | 30.0 | 14.3 |
| 0.100 | 40.0 | 16.7 |
| 0.200 | 48.0 | 18.2 |
| 0.500 | 54.6 | 19.3 |
| 1.000 | 57.2 | 19.7 |
| 2.000 | 58.6 | 19.9 |
| 5.000 | 59.5 | 20.0 |
| 10.000 | 59.8 | 20.0 |
| 20.000 | 59.9 | 20.0 |
| 50.000 | 60.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect eco-competitive Incorrect homo-competitive Incorrect non-competitive Incorrect un-competitive Correct MC273e_fbe1
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 40.0 | 20.0 |
| 0.002 | 60.0 | 30.0 |
| 0.005 | 85.8 | 42.9 |
| 0.010 | 100.0 | 50.0 |
| 0.020 | 109.1 | 54.6 |
| 0.050 | 115.4 | 57.7 |
| 0.100 | 117.7 | 58.9 |
| 0.200 | 118.9 | 59.5 |
| 0.500 | 119.6 | 59.8 |
| 1.000 | 119.8 | 59.9 |
| 2.000 | 119.9 | 60.0 |
| 5.000 | 120.0 | 60.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Correct poly-competitive Incorrect ultra-competitive Incorrect un-competitive Incorrect MCf001_9fd5
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 5.5 | 3.7 |
| 0.002 | 10.0 | 6.7 |
| 0.005 | 20.0 | 13.4 |
| 0.010 | 30.0 | 20.0 |
| 0.020 | 40.0 | 26.7 |
| 0.050 | 50.0 | 33.4 |
| 0.100 | 54.6 | 36.4 |
| 0.200 | 57.2 | 38.1 |
| 0.500 | 58.9 | 39.3 |
| 1.000 | 59.5 | 39.7 |
| 2.000 | 59.8 | 39.9 |
| 5.000 | 59.9 | 40.0 |
| 10.000 | 60.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
auto-competitive Incorrect competitive Incorrect non-competitive Correct semi-competitive Incorrect un-competitive Incorrect MCcf9f_e464
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 13.4 | 13.4 |
| 0.002 | 22.9 | 20.0 |
| 0.005 | 40.0 | 28.6 |
| 0.010 | 53.4 | 33.4 |
| 0.020 | 64.0 | 36.4 |
| 0.050 | 72.8 | 38.5 |
| 0.100 | 76.2 | 39.3 |
| 0.200 | 78.1 | 39.7 |
| 0.500 | 79.3 | 39.9 |
| 1.000 | 79.7 | 40.0 |
| 2.000 | 79.9 | 40.0 |
| 5.000 | 80.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect contra-competitive Incorrect non-competitive Incorrect semi-competitive Incorrect un-competitive Correct MC887a_2296
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 23.4 | 20.0 |
| 0.002 | 40.0 | 30.0 |
| 0.005 | 70.0 | 42.9 |
| 0.010 | 93.4 | 50.0 |
| 0.020 | 112.0 | 54.6 |
| 0.050 | 127.3 | 57.7 |
| 0.100 | 133.4 | 58.9 |
| 0.200 | 136.6 | 59.5 |
| 0.500 | 138.7 | 59.8 |
| 1.000 | 139.4 | 59.9 |
| 2.000 | 139.7 | 60.0 |
| 5.000 | 139.9 | 60.0 |
| 10.000 | 140.0 | 60.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect extra-competitive Incorrect homo-competitive Incorrect non-competitive Incorrect un-competitive Correct MC7008_947c
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 46.7 | 40.0 |
| 0.002 | 70.0 | 53.4 |
| 0.005 | 100.1 | 66.7 |
| 0.010 | 116.7 | 72.8 |
| 0.020 | 127.3 | 76.2 |
| 0.050 | 134.7 | 78.5 |
| 0.100 | 137.3 | 79.3 |
| 0.200 | 138.7 | 79.7 |
| 0.500 | 139.5 | 79.9 |
| 1.000 | 139.8 | 80.0 |
| 2.000 | 139.9 | 80.0 |
| 5.000 | 140.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Incorrect omni-competitive Incorrect quasi-competitive Incorrect un-competitive Correct MCaf5c_bc4d
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 2.9 | 1.0 |
| 0.002 | 5.5 | 1.9 |
| 0.005 | 12.0 | 4.0 |
| 0.010 | 20.0 | 6.7 |
| 0.020 | 30.0 | 10.0 |
| 0.050 | 42.9 | 14.3 |
| 0.100 | 50.0 | 16.7 |
| 0.200 | 54.6 | 18.2 |
| 0.500 | 57.7 | 19.3 |
| 1.000 | 58.9 | 19.7 |
| 2.000 | 59.5 | 19.9 |
| 5.000 | 59.8 | 20.0 |
| 10.000 | 59.9 | 20.0 |
| 20.000 | 60.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect inter-competitive Incorrect non-competitive Correct self-competitive Incorrect un-competitive Incorrect MCf242_d959
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 8.6 | 6.7 |
| 0.002 | 16.4 | 12.8 |
| 0.005 | 36.0 | 28.0 |
| 0.010 | 60.1 | 46.7 |
| 0.020 | 90.0 | 70.0 |
| 0.050 | 128.6 | 100.0 |
| 0.100 | 150.0 | 116.7 |
| 0.200 | 163.7 | 127.3 |
| 0.500 | 173.1 | 134.7 |
| 1.000 | 176.5 | 137.3 |
| 2.000 | 178.3 | 138.7 |
| 5.000 | 179.3 | 139.5 |
| 10.000 | 179.7 | 139.8 |
| 20.000 | 179.9 | 139.9 |
| 50.000 | 180.0 | 140.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect extra-competitive Incorrect non-competitive Correct oligo-competitive Incorrect un-competitive Incorrect MC8001_985e
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 7.7 | 7.3 |
| 0.002 | 14.6 | 13.4 |
| 0.005 | 32.0 | 26.7 |
| 0.010 | 53.4 | 40.0 |
| 0.020 | 80.0 | 53.4 |
| 0.050 | 114.3 | 66.7 |
| 0.100 | 133.4 | 72.8 |
| 0.200 | 145.5 | 76.2 |
| 0.500 | 153.9 | 78.5 |
| 1.000 | 156.9 | 79.3 |
| 2.000 | 158.5 | 79.7 |
| 5.000 | 159.4 | 79.9 |
| 10.000 | 159.7 | 80.0 |
| 20.000 | 159.9 | 80.0 |
| 50.000 | 160.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
auto-competitive Incorrect competitive Incorrect non-competitive Incorrect over-competitive Incorrect un-competitive Correct MC5425_6ddd
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 3.2 | 2.9 |
| 0.002 | 6.2 | 5.5 |
| 0.005 | 14.6 | 12.0 |
| 0.010 | 26.7 | 20.0 |
| 0.020 | 45.8 | 30.0 |
| 0.050 | 80.0 | 42.9 |
| 0.100 | 106.7 | 50.0 |
| 0.200 | 128.0 | 54.6 |
| 0.500 | 145.5 | 57.7 |
| 1.000 | 152.4 | 58.9 |
| 2.000 | 156.1 | 59.5 |
| 5.000 | 158.5 | 59.8 |
| 10.000 | 159.3 | 59.9 |
| 20.000 | 159.7 | 60.0 |
| 50.000 | 159.9 | 60.0 |
| 100.000 | 160.0 | 60.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect epi-competitive Incorrect hyper-competitive Incorrect non-competitive Incorrect un-competitive Correct MCc234_bd1f
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 9.1 | 6.7 |
| 0.002 | 16.7 | 11.5 |
| 0.005 | 33.4 | 20.0 |
| 0.010 | 50.0 | 26.7 |
| 0.020 | 66.7 | 32.0 |
| 0.050 | 83.4 | 36.4 |
| 0.100 | 91.0 | 38.1 |
| 0.200 | 95.3 | 39.1 |
| 0.500 | 98.1 | 39.7 |
| 1.000 | 99.1 | 39.9 |
| 2.000 | 99.6 | 40.0 |
| 5.000 | 99.9 | 40.0 |
| 10.000 | 100.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect hetero-competitive Incorrect non-competitive Incorrect ortho-competitive Incorrect un-competitive Correct MC1f55_0b9e
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 4.8 | 3.7 |
| 0.002 | 9.1 | 6.7 |
| 0.005 | 20.0 | 13.4 |
| 0.010 | 33.4 | 20.0 |
| 0.020 | 50.0 | 26.7 |
| 0.050 | 71.5 | 33.4 |
| 0.100 | 83.4 | 36.4 |
| 0.200 | 91.0 | 38.1 |
| 0.500 | 96.2 | 39.3 |
| 1.000 | 98.1 | 39.7 |
| 2.000 | 99.1 | 39.9 |
| 5.000 | 99.7 | 40.0 |
| 10.000 | 99.9 | 40.0 |
| 20.000 | 100.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect dis-competitive Incorrect hetero-competitive Incorrect non-competitive Incorrect un-competitive Correct MC09b7_9f0b
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 18.2 | 16.7 |
| 0.002 | 33.4 | 28.6 |
| 0.005 | 66.7 | 50.0 |
| 0.010 | 100.0 | 66.7 |
| 0.020 | 133.4 | 80.0 |
| 0.050 | 166.7 | 91.0 |
| 0.100 | 181.9 | 95.3 |
| 0.200 | 190.5 | 97.6 |
| 0.500 | 196.1 | 99.1 |
| 1.000 | 198.1 | 99.6 |
| 2.000 | 199.1 | 99.8 |
| 5.000 | 199.7 | 100.0 |
| 10.000 | 199.9 | 100.0 |
| 20.000 | 200.0 | 100.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Incorrect omni-competitive Incorrect post-competitive Incorrect un-competitive Correct MC6561_6daf
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 33.4 | 20.0 |
| 0.002 | 50.0 | 26.7 |
| 0.005 | 71.5 | 33.4 |
| 0.010 | 83.4 | 36.4 |
| 0.020 | 91.0 | 38.1 |
| 0.050 | 96.2 | 39.3 |
| 0.100 | 98.1 | 39.7 |
| 0.200 | 99.1 | 39.9 |
| 0.500 | 99.7 | 40.0 |
| 1.000 | 99.9 | 40.0 |
| 2.000 | 100.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect dis-competitive Incorrect non-competitive Incorrect ultra-competitive Incorrect un-competitive Correct MC607c_ea35
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 0.8 | 1.0 |
| 0.002 | 1.6 | 1.9 |
| 0.005 | 3.7 | 4.0 |
| 0.010 | 6.7 | 6.7 |
| 0.020 | 11.5 | 10.0 |
| 0.050 | 20.0 | 14.3 |
| 0.100 | 26.7 | 16.7 |
| 0.200 | 32.0 | 18.2 |
| 0.500 | 36.4 | 19.3 |
| 1.000 | 38.1 | 19.7 |
| 2.000 | 39.1 | 19.9 |
| 5.000 | 39.7 | 20.0 |
| 10.000 | 39.9 | 20.0 |
| 20.000 | 40.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Incorrect ortho-competitive Incorrect pre-competitive Incorrect un-competitive Correct MC813e_2eba
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 2.8 | 0.7 |
| 0.002 | 5.4 | 1.4 |
| 0.005 | 12.8 | 3.5 |
| 0.010 | 23.4 | 6.7 |
| 0.020 | 40.0 | 12.8 |
| 0.050 | 70.0 | 28.0 |
| 0.100 | 93.4 | 46.7 |
| 0.200 | 112.0 | 70.0 |
| 0.500 | 127.3 | 100.0 |
| 1.000 | 133.4 | 116.7 |
| 2.000 | 136.6 | 127.3 |
| 5.000 | 138.7 | 134.7 |
| 10.000 | 139.4 | 137.3 |
| 20.000 | 139.7 | 138.7 |
| 50.000 | 139.9 | 139.5 |
| 100.000 | 140.0 | 139.8 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct non-competitive Incorrect ortho-competitive Incorrect over-competitive Incorrect un-competitive Incorrect MC9f57_1ace
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 14.6 | 3.2 |
| 0.002 | 26.7 | 6.2 |
| 0.005 | 53.4 | 14.6 |
| 0.010 | 80.0 | 26.7 |
| 0.020 | 106.7 | 45.8 |
| 0.050 | 133.4 | 80.0 |
| 0.100 | 145.5 | 106.7 |
| 0.200 | 152.4 | 128.0 |
| 0.500 | 156.9 | 145.5 |
| 1.000 | 158.5 | 152.4 |
| 2.000 | 159.3 | 156.1 |
| 5.000 | 159.7 | 158.5 |
| 10.000 | 159.9 | 159.3 |
| 20.000 | 160.0 | 159.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct dis-competitive Incorrect idio-competitive Incorrect non-competitive Incorrect un-competitive Incorrect MCc90d_bbd7
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 60.0 | 3.6 |
| 0.002 | 90.0 | 7.0 |
| 0.005 | 128.6 | 16.4 |
| 0.010 | 150.0 | 30.0 |
| 0.020 | 163.7 | 51.5 |
| 0.050 | 173.1 | 90.0 |
| 0.100 | 176.5 | 120.0 |
| 0.200 | 178.3 | 144.0 |
| 0.500 | 179.3 | 163.7 |
| 1.000 | 179.7 | 171.5 |
| 2.000 | 179.9 | 175.7 |
| 5.000 | 180.0 | 178.3 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct non-competitive Incorrect oligo-competitive Incorrect omni-competitive Incorrect un-competitive Incorrect MC478f_c91f
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 3.7 | 1.9 |
| 0.002 | 6.7 | 3.4 |
| 0.005 | 13.4 | 6.7 |
| 0.010 | 20.0 | 10.0 |
| 0.020 | 26.7 | 13.4 |
| 0.050 | 33.4 | 16.7 |
| 0.100 | 36.4 | 18.2 |
| 0.200 | 38.1 | 19.1 |
| 0.500 | 39.3 | 19.7 |
| 1.000 | 39.7 | 19.9 |
| 2.000 | 39.9 | 20.0 |
| 5.000 | 40.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect extra-competitive Incorrect non-competitive Correct over-competitive Incorrect un-competitive Incorrect MC211b_9e0d
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 2.0 | 0.8 |
| 0.002 | 3.9 | 1.6 |
| 0.005 | 9.1 | 3.7 |
| 0.010 | 16.7 | 6.7 |
| 0.020 | 28.6 | 11.5 |
| 0.050 | 50.0 | 20.0 |
| 0.100 | 66.7 | 26.7 |
| 0.200 | 80.0 | 32.0 |
| 0.500 | 91.0 | 36.4 |
| 1.000 | 95.3 | 38.1 |
| 2.000 | 97.6 | 39.1 |
| 5.000 | 99.1 | 39.7 |
| 10.000 | 99.6 | 39.9 |
| 20.000 | 99.8 | 40.0 |
| 50.000 | 100.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect dis-competitive Incorrect non-competitive Correct self-competitive Incorrect un-competitive Incorrect MC2357_9bb3
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 9.1 | 1.9 |
| 0.002 | 16.7 | 3.4 |
| 0.005 | 33.4 | 6.7 |
| 0.010 | 50.0 | 10.0 |
| 0.020 | 66.7 | 13.4 |
| 0.050 | 83.4 | 16.7 |
| 0.100 | 91.0 | 18.2 |
| 0.200 | 95.3 | 19.1 |
| 0.500 | 98.1 | 19.7 |
| 1.000 | 99.1 | 19.9 |
| 2.000 | 99.6 | 20.0 |
| 5.000 | 99.9 | 20.0 |
| 10.000 | 100.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Correct over-competitive Incorrect ultra-competitive Incorrect un-competitive Incorrect MC03b8_2d9c
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 66.7 | 0.1 |
| 0.002 | 100.0 | 0.1 |
| 0.005 | 142.9 | 0.1 |
| 0.010 | 166.7 | 0.2 |
| 0.020 | 181.9 | 0.4 |
| 0.050 | 192.4 | 1.0 |
| 0.100 | 196.1 | 2.0 |
| 0.200 | 198.1 | 4.0 |
| 0.500 | 199.3 | 9.6 |
| 1.000 | 199.7 | 18.2 |
| 2.000 | 199.9 | 33.4 |
| 5.000 | 200.0 | 66.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct mis-competitive Incorrect non-competitive Incorrect pre-competitive Incorrect un-competitive Incorrect MC3a38_71a9
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 26.7 | 20.0 |
| 0.002 | 45.8 | 30.0 |
| 0.005 | 80.0 | 42.9 |
| 0.010 | 106.7 | 50.0 |
| 0.020 | 128.0 | 54.6 |
| 0.050 | 145.5 | 57.7 |
| 0.100 | 152.4 | 58.9 |
| 0.200 | 156.1 | 59.5 |
| 0.500 | 158.5 | 59.8 |
| 1.000 | 159.3 | 59.9 |
| 2.000 | 159.7 | 60.0 |
| 5.000 | 159.9 | 60.0 |
| 10.000 | 160.0 | 60.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect hetero-competitive Incorrect non-competitive Incorrect ultra-competitive Incorrect un-competitive Correct MC4caf_985e
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 66.7 | 50.0 |
| 0.002 | 100.0 | 66.7 |
| 0.005 | 142.9 | 83.4 |
| 0.010 | 166.7 | 91.0 |
| 0.020 | 181.9 | 95.3 |
| 0.050 | 192.4 | 98.1 |
| 0.100 | 196.1 | 99.1 |
| 0.200 | 198.1 | 99.6 |
| 0.500 | 199.3 | 99.9 |
| 1.000 | 199.7 | 100.0 |
| 2.000 | 199.9 | 100.0 |
| 5.000 | 200.0 | 100.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
auto-competitive Incorrect competitive Incorrect non-competitive Incorrect over-competitive Incorrect un-competitive Correct MCb038_18a1
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 53.4 | 0.2 |
| 0.002 | 80.0 | 0.4 |
| 0.005 | 114.3 | 0.8 |
| 0.010 | 133.4 | 1.6 |
| 0.020 | 145.5 | 3.2 |
| 0.050 | 153.9 | 7.7 |
| 0.100 | 156.9 | 14.6 |
| 0.200 | 158.5 | 26.7 |
| 0.500 | 159.4 | 53.4 |
| 1.000 | 159.7 | 80.0 |
| 2.000 | 159.9 | 106.7 |
| 5.000 | 160.0 | 133.4 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct intra-competitive Incorrect non-competitive Incorrect semi-competitive Incorrect un-competitive Incorrect MC1e22_811d
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 16.4 | 0.1 |
| 0.002 | 30.0 | 0.2 |
| 0.005 | 60.1 | 0.5 |
| 0.010 | 90.0 | 0.9 |
| 0.020 | 120.1 | 1.8 |
| 0.050 | 150.0 | 4.4 |
| 0.100 | 163.7 | 8.6 |
| 0.200 | 171.5 | 16.4 |
| 0.500 | 176.5 | 36.0 |
| 1.000 | 178.3 | 60.0 |
| 2.000 | 179.2 | 90.0 |
| 5.000 | 179.7 | 128.6 |
| 10.000 | 179.9 | 150.0 |
| 20.000 | 180.0 | 163.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct inter-competitive Incorrect non-competitive Incorrect pseudo-competitive Incorrect un-competitive Incorrect MC3a78_76b1
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 33.4 | 26.7 |
| 0.002 | 57.2 | 40.0 |
| 0.005 | 100.0 | 57.2 |
| 0.010 | 133.4 | 66.7 |
| 0.020 | 160.0 | 72.8 |
| 0.050 | 181.9 | 77.0 |
| 0.100 | 190.5 | 78.5 |
| 0.200 | 195.2 | 79.3 |
| 0.500 | 198.1 | 79.7 |
| 1.000 | 199.1 | 79.9 |
| 2.000 | 199.6 | 80.0 |
| 5.000 | 199.9 | 80.0 |
| 10.000 | 200.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect idio-competitive Incorrect non-competitive Incorrect proto-competitive Incorrect un-competitive Correct MC45f5_9c5d
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 26.7 | 20.0 |
| 0.002 | 40.0 | 26.7 |
| 0.005 | 57.2 | 33.4 |
| 0.010 | 66.7 | 36.4 |
| 0.020 | 72.8 | 38.1 |
| 0.050 | 77.0 | 39.3 |
| 0.100 | 78.5 | 39.7 |
| 0.200 | 79.3 | 39.9 |
| 0.500 | 79.7 | 40.0 |
| 1.000 | 79.9 | 40.0 |
| 2.000 | 80.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect epi-competitive Incorrect hetero-competitive Incorrect non-competitive Incorrect un-competitive Correct MC502e_66f4
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 7.3 | 1.6 |
| 0.002 | 13.4 | 3.1 |
| 0.005 | 26.7 | 7.3 |
| 0.010 | 40.0 | 13.4 |
| 0.020 | 53.4 | 22.9 |
| 0.050 | 66.7 | 40.0 |
| 0.100 | 72.8 | 53.4 |
| 0.200 | 76.2 | 64.0 |
| 0.500 | 78.5 | 72.8 |
| 1.000 | 79.3 | 76.2 |
| 2.000 | 79.7 | 78.1 |
| 5.000 | 79.9 | 79.3 |
| 10.000 | 80.0 | 79.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct iso-competitive Incorrect non-competitive Incorrect proto-competitive Incorrect un-competitive Incorrect MC831f_89c0
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 6.7 | 7.3 |
| 0.002 | 12.8 | 13.4 |
| 0.005 | 28.0 | 26.7 |
| 0.010 | 46.7 | 40.0 |
| 0.020 | 70.0 | 53.4 |
| 0.050 | 100.0 | 66.7 |
| 0.100 | 116.7 | 72.8 |
| 0.200 | 127.3 | 76.2 |
| 0.500 | 134.7 | 78.5 |
| 1.000 | 137.3 | 79.3 |
| 2.000 | 138.7 | 79.7 |
| 5.000 | 139.5 | 79.9 |
| 10.000 | 139.8 | 80.0 |
| 20.000 | 139.9 | 80.0 |
| 50.000 | 140.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect hetero-competitive Incorrect hypo-competitive Incorrect non-competitive Incorrect un-competitive Correct MCc516_e40b
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 9.6 | 4.0 |
| 0.002 | 18.2 | 7.7 |
| 0.005 | 40.0 | 18.2 |
| 0.010 | 66.7 | 33.4 |
| 0.020 | 100.0 | 57.2 |
| 0.050 | 142.9 | 100.0 |
| 0.100 | 166.7 | 133.4 |
| 0.200 | 181.9 | 160.0 |
| 0.500 | 192.4 | 181.9 |
| 1.000 | 196.1 | 190.5 |
| 2.000 | 198.1 | 195.2 |
| 5.000 | 199.3 | 198.1 |
| 10.000 | 199.7 | 199.1 |
| 20.000 | 199.9 | 199.6 |
| 50.000 | 200.0 | 199.9 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct homo-competitive Incorrect non-competitive Incorrect ultra-competitive Incorrect un-competitive Incorrect MC20ff_2ec4
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 1.2 | 0.8 |
| 0.002 | 2.4 | 1.6 |
| 0.005 | 5.5 | 3.7 |
| 0.010 | 10.0 | 6.7 |
| 0.020 | 17.2 | 11.5 |
| 0.050 | 30.0 | 20.0 |
| 0.100 | 40.0 | 26.7 |
| 0.200 | 48.0 | 32.0 |
| 0.500 | 54.6 | 36.4 |
| 1.000 | 57.2 | 38.1 |
| 2.000 | 58.6 | 39.1 |
| 5.000 | 59.5 | 39.7 |
| 10.000 | 59.8 | 39.9 |
| 20.000 | 59.9 | 40.0 |
| 50.000 | 60.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
anti-competitive Incorrect competitive Incorrect non-competitive Correct supra-competitive Incorrect un-competitive Incorrect MC5cbf_73d2
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 16.7 | 13.4 |
| 0.002 | 28.6 | 20.0 |
| 0.005 | 50.0 | 28.6 |
| 0.010 | 66.7 | 33.4 |
| 0.020 | 80.0 | 36.4 |
| 0.050 | 91.0 | 38.5 |
| 0.100 | 95.3 | 39.3 |
| 0.200 | 97.6 | 39.7 |
| 0.500 | 99.1 | 39.9 |
| 1.000 | 99.6 | 40.0 |
| 2.000 | 99.8 | 40.0 |
| 5.000 | 100.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect extra-competitive Incorrect non-competitive Incorrect quasi-competitive Incorrect un-competitive Correct MCdebd_83e0
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 30.0 | 26.7 |
| 0.002 | 51.5 | 40.0 |
| 0.005 | 90.0 | 57.2 |
| 0.010 | 120.1 | 66.7 |
| 0.020 | 144.0 | 72.8 |
| 0.050 | 163.7 | 77.0 |
| 0.100 | 171.5 | 78.5 |
| 0.200 | 175.7 | 79.3 |
| 0.500 | 178.3 | 79.7 |
| 1.000 | 179.2 | 79.9 |
| 2.000 | 179.6 | 80.0 |
| 5.000 | 179.9 | 80.0 |
| 10.000 | 180.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect hetero-competitive Incorrect homo-competitive Incorrect non-competitive Incorrect un-competitive Correct MC9801_11bc
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 4.8 | 2.0 |
| 0.002 | 9.1 | 3.7 |
| 0.005 | 20.0 | 8.0 |
| 0.010 | 33.4 | 13.4 |
| 0.020 | 50.0 | 20.0 |
| 0.050 | 71.5 | 28.6 |
| 0.100 | 83.4 | 33.4 |
| 0.200 | 91.0 | 36.4 |
| 0.500 | 96.2 | 38.5 |
| 1.000 | 98.1 | 39.3 |
| 2.000 | 99.1 | 39.7 |
| 5.000 | 99.7 | 39.9 |
| 10.000 | 99.9 | 40.0 |
| 20.000 | 100.0 | 40.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Correct para-competitive Incorrect super-competitive Incorrect un-competitive Incorrect MC288c_47f5
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 2.4 | 0.4 |
| 0.002 | 4.7 | 0.8 |
| 0.005 | 11.0 | 1.9 |
| 0.010 | 20.0 | 3.4 |
| 0.020 | 34.3 | 5.8 |
| 0.050 | 60.0 | 10.0 |
| 0.100 | 80.0 | 13.4 |
| 0.200 | 96.0 | 16.0 |
| 0.500 | 109.1 | 18.2 |
| 1.000 | 114.3 | 19.1 |
| 2.000 | 117.1 | 19.6 |
| 5.000 | 118.9 | 19.9 |
| 10.000 | 119.5 | 20.0 |
| 20.000 | 119.8 | 20.0 |
| 50.000 | 119.9 | 20.0 |
| 100.000 | 120.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Correct post-competitive Incorrect quasi-competitive Incorrect un-competitive Incorrect MC182b_be99
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 11.0 | 7.3 |
| 0.002 | 20.0 | 13.4 |
| 0.005 | 40.0 | 26.7 |
| 0.010 | 60.0 | 40.0 |
| 0.020 | 80.0 | 53.4 |
| 0.050 | 100.0 | 66.7 |
| 0.100 | 109.1 | 72.8 |
| 0.200 | 114.3 | 76.2 |
| 0.500 | 117.7 | 78.5 |
| 1.000 | 118.9 | 79.3 |
| 2.000 | 119.5 | 79.7 |
| 5.000 | 119.8 | 79.9 |
| 10.000 | 119.9 | 80.0 |
| 20.000 | 120.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Correct poly-competitive Incorrect proto-competitive Incorrect un-competitive Incorrect MC5646_1170
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 4.0 | 0.1 |
| 0.002 | 7.7 | 0.1 |
| 0.005 | 18.2 | 0.1 |
| 0.010 | 33.4 | 0.1 |
| 0.020 | 57.2 | 0.2 |
| 0.050 | 100.0 | 0.5 |
| 0.100 | 133.4 | 1.0 |
| 0.200 | 160.0 | 2.0 |
| 0.500 | 181.9 | 4.9 |
| 1.000 | 190.5 | 9.6 |
| 2.000 | 195.2 | 18.2 |
| 5.000 | 198.1 | 40.0 |
| 10.000 | 199.1 | 66.7 |
| 20.000 | 199.6 | 100.0 |
| 50.000 | 199.9 | 142.9 |
| 100.000 | 200.0 | 166.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
anti-competitive Incorrect competitive Correct non-competitive Incorrect ultra-competitive Incorrect un-competitive Incorrect MC8136_b7de
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 2.0 | 1.0 |
| 0.002 | 3.9 | 2.0 |
| 0.005 | 9.1 | 4.8 |
| 0.010 | 16.7 | 9.1 |
| 0.020 | 28.6 | 16.7 |
| 0.050 | 50.0 | 33.4 |
| 0.100 | 66.7 | 50.0 |
| 0.200 | 80.0 | 66.7 |
| 0.500 | 91.0 | 83.4 |
| 1.000 | 95.3 | 91.0 |
| 2.000 | 97.6 | 95.3 |
| 5.000 | 99.1 | 98.1 |
| 10.000 | 99.6 | 99.1 |
| 20.000 | 99.8 | 99.6 |
| 50.000 | 100.0 | 99.9 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct hetero-competitive Incorrect mis-competitive Incorrect non-competitive Incorrect un-competitive Incorrect MC91b5_ebe1
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 9.1 | 4.8 |
| 0.002 | 16.7 | 9.1 |
| 0.005 | 33.4 | 20.0 |
| 0.010 | 50.0 | 33.4 |
| 0.020 | 66.7 | 50.0 |
| 0.050 | 83.4 | 71.5 |
| 0.100 | 91.0 | 83.4 |
| 0.200 | 95.3 | 91.0 |
| 0.500 | 98.1 | 96.2 |
| 1.000 | 99.1 | 98.1 |
| 2.000 | 99.6 | 99.1 |
| 5.000 | 99.9 | 99.7 |
| 10.000 | 100.0 | 99.9 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Correct non-competitive Incorrect quasi-competitive Incorrect ultra-competitive Incorrect un-competitive Incorrect MC6690_cd89
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 3.6 | 1.6 |
| 0.002 | 7.0 | 3.1 |
| 0.005 | 16.4 | 7.3 |
| 0.010 | 30.0 | 13.4 |
| 0.020 | 51.5 | 22.9 |
| 0.050 | 90.0 | 40.0 |
| 0.100 | 120.0 | 53.4 |
| 0.200 | 144.0 | 64.0 |
| 0.500 | 163.7 | 72.8 |
| 1.000 | 171.5 | 76.2 |
| 2.000 | 175.7 | 78.1 |
| 5.000 | 178.3 | 79.3 |
| 10.000 | 179.2 | 79.7 |
| 20.000 | 179.6 | 79.9 |
| 50.000 | 179.9 | 80.0 |
| 100.000 | 180.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect dis-competitive Incorrect non-competitive Correct para-competitive Incorrect un-competitive Incorrect MC42fe_9c5d
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 8.6 | 7.3 |
| 0.002 | 16.4 | 13.4 |
| 0.005 | 36.0 | 26.7 |
| 0.010 | 60.1 | 40.0 |
| 0.020 | 90.0 | 53.4 |
| 0.050 | 128.6 | 66.7 |
| 0.100 | 150.0 | 72.8 |
| 0.200 | 163.7 | 76.2 |
| 0.500 | 173.1 | 78.5 |
| 1.000 | 176.5 | 79.3 |
| 2.000 | 178.3 | 79.7 |
| 5.000 | 179.3 | 79.9 |
| 10.000 | 179.7 | 80.0 |
| 20.000 | 179.9 | 80.0 |
| 50.000 | 180.0 | 80.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect epi-competitive Incorrect hetero-competitive Incorrect non-competitive Incorrect un-competitive Correct MCabb3_2d58
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.001 | 46.7 | 40.0 |
| 0.002 | 70.0 | 60.0 |
| 0.005 | 100.1 | 85.8 |
| 0.010 | 116.7 | 100.0 |
| 0.020 | 127.3 | 109.1 |
| 0.050 | 134.7 | 115.4 |
| 0.100 | 137.3 | 117.7 |
| 0.200 | 138.7 | 118.9 |
| 0.500 | 139.5 | 119.6 |
| 1.000 | 139.8 | 119.8 |
| 2.000 | 139.9 | 119.9 |
| 5.000 | 140.0 | 120.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
competitive Incorrect non-competitive Correct semi-competitive Incorrect ultra-competitive Incorrect un-competitive Incorrect