MC
963b_c402
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 | 40.0 | 0.1 |
| 0.005 | 57.2 | 0.2 |
| 0.010 | 66.7 | 0.4 |
| 0.020 | 72.8 | 0.8 |
| 0.050 | 77.0 | 2.0 |
| 0.100 | 78.5 | 3.9 |
| 0.200 | 79.3 | 7.3 |
| 0.500 | 79.7 | 16.0 |
| 1.000 | 79.9 | 26.7 |
| 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 Correct hypo-competitive Incorrect non-competitive Incorrect pseudo-competitive Incorrect un-competitive Incorrect MCd552_6ed4
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 | 6.7 |
| 0.002 | 60.0 | 10.0 |
| 0.005 | 85.8 | 14.3 |
| 0.010 | 100.0 | 16.7 |
| 0.020 | 109.1 | 18.2 |
| 0.050 | 115.4 | 19.3 |
| 0.100 | 117.7 | 19.7 |
| 0.200 | 118.9 | 19.9 |
| 0.500 | 119.6 | 20.0 |
| 1.000 | 119.8 | 20.0 |
| 2.000 | 119.9 | 20.0 |
| 5.000 | 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 extra-competitive Incorrect non-competitive Correct ortho-competitive Incorrect un-competitive Incorrect MC08ae_f0ab
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 iso-competitive Incorrect non-competitive Incorrect un-competitive Correct MC3484_28d7
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 | 0.6 |
| 0.002 | 2.4 | 1.2 |
| 0.005 | 5.5 | 2.9 |
| 0.010 | 10.0 | 5.5 |
| 0.020 | 17.2 | 10.0 |
| 0.050 | 30.0 | 20.0 |
| 0.100 | 40.0 | 30.0 |
| 0.200 | 48.0 | 40.0 |
| 0.500 | 54.6 | 50.0 |
| 1.000 | 57.2 | 54.6 |
| 2.000 | 58.6 | 57.2 |
| 5.000 | 59.5 | 58.9 |
| 10.000 | 59.8 | 59.5 |
| 20.000 | 59.9 | 59.8 |
| 50.000 | 60.0 | 59.9 |
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 dis-competitive Incorrect non-competitive Incorrect proto-competitive Incorrect un-competitive Incorrect MC0f0d_a030
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 | 1.2 |
| 0.002 | 30.0 | 2.4 |
| 0.005 | 42.9 | 5.5 |
| 0.010 | 50.0 | 10.0 |
| 0.020 | 54.6 | 17.2 |
| 0.050 | 57.7 | 30.0 |
| 0.100 | 58.9 | 40.0 |
| 0.200 | 59.5 | 48.0 |
| 0.500 | 59.8 | 54.6 |
| 1.000 | 59.9 | 57.2 |
| 2.000 | 60.0 | 58.6 |
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 non-competitive Incorrect post-competitive Incorrect super-competitive Incorrect un-competitive Incorrect MCe071_1e1f
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 | 0.1 |
| 0.100 | 26.7 | 0.2 |
| 0.200 | 32.0 | 0.4 |
| 0.500 | 36.4 | 1.0 |
| 1.000 | 38.1 | 2.0 |
| 2.000 | 39.1 | 3.7 |
| 5.000 | 39.7 | 8.0 |
| 10.000 | 39.9 | 13.4 |
| 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 Correct mis-competitive Incorrect non-competitive Incorrect supra-competitive Incorrect un-competitive Incorrect MC2552_c95a
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 | 0.3 |
| 0.002 | 40.0 | 0.6 |
| 0.005 | 70.0 | 1.4 |
| 0.010 | 93.4 | 2.8 |
| 0.020 | 112.0 | 5.4 |
| 0.050 | 127.3 | 12.8 |
| 0.100 | 133.4 | 23.4 |
| 0.200 | 136.6 | 40.0 |
| 0.500 | 138.7 | 70.0 |
| 1.000 | 139.4 | 93.4 |
| 2.000 | 139.7 | 112.0 |
| 5.000 | 139.9 | 127.3 |
| 10.000 | 140.0 | 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]).
anti-competitive Incorrect competitive Correct extra-competitive Incorrect non-competitive Incorrect un-competitive Incorrect MC1c0d_a69b
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 | 2.0 |
| 0.002 | 7.3 | 3.7 |
| 0.005 | 16.0 | 8.0 |
| 0.010 | 26.7 | 13.4 |
| 0.020 | 40.0 | 20.0 |
| 0.050 | 57.2 | 28.6 |
| 0.100 | 66.7 | 33.4 |
| 0.200 | 72.8 | 36.4 |
| 0.500 | 77.0 | 38.5 |
| 1.000 | 78.5 | 39.3 |
| 2.000 | 79.3 | 39.7 |
| 5.000 | 79.7 | 39.9 |
| 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 extra-competitive Incorrect non-competitive Correct para-competitive Incorrect un-competitive Incorrect MC8018_e57b
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 | 2.0 |
| 0.002 | 5.4 | 3.9 |
| 0.005 | 12.8 | 9.1 |
| 0.010 | 23.4 | 16.7 |
| 0.020 | 40.0 | 28.6 |
| 0.050 | 70.0 | 50.0 |
| 0.100 | 93.4 | 66.7 |
| 0.200 | 112.0 | 80.0 |
| 0.500 | 127.3 | 91.0 |
| 1.000 | 133.4 | 95.3 |
| 2.000 | 136.6 | 97.6 |
| 5.000 | 138.7 | 99.1 |
| 10.000 | 139.4 | 99.6 |
| 20.000 | 139.7 | 99.8 |
| 50.000 | 139.9 | 100.0 |
| 100.000 | 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 iso-competitive Incorrect non-competitive Correct over-competitive Incorrect un-competitive Incorrect MC64dc_05f2
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 iso-competitive Incorrect non-competitive Correct pre-competitive Incorrect un-competitive Incorrect MCdebd_897a
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 non-competitive Incorrect omni-competitive Incorrect ortho-competitive Incorrect un-competitive Correct MCe016_4990
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 non-competitive Correct para-competitive Incorrect pre-competitive Incorrect un-competitive Incorrect MCc234_521b
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 dis-competitive Incorrect non-competitive Incorrect supra-competitive Incorrect un-competitive Correct MC0014_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 | 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 contra-competitive Incorrect iso-competitive Incorrect non-competitive Incorrect un-competitive Correct MC8268_8103
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 non-competitive Correct oligo-competitive Incorrect post-competitive Incorrect un-competitive Incorrect MCa038_5a1e
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 | 5.5 |
| 0.002 | 13.4 | 10.0 |
| 0.005 | 26.7 | 20.0 |
| 0.010 | 40.0 | 30.0 |
| 0.020 | 53.4 | 40.0 |
| 0.050 | 66.7 | 50.0 |
| 0.100 | 72.8 | 54.6 |
| 0.200 | 76.2 | 57.2 |
| 0.500 | 78.5 | 58.9 |
| 1.000 | 79.3 | 59.5 |
| 2.000 | 79.7 | 59.8 |
| 5.000 | 79.9 | 59.9 |
| 10.000 | 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 hypo-competitive Incorrect non-competitive Correct post-competitive Incorrect un-competitive Incorrect MC7b8a_6400
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]).
competitive Incorrect hypo-competitive Incorrect non-competitive Incorrect over-competitive Incorrect un-competitive Correct MC478f_be33
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 non-competitive Correct oligo-competitive Incorrect ultra-competitive Incorrect un-competitive Incorrect MC3a38_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 | 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 idio-competitive Incorrect non-competitive Incorrect supra-competitive Incorrect un-competitive Correct MCcac7_ee3d
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]).
competitive Incorrect extra-competitive Incorrect hetero-competitive Incorrect non-competitive Incorrect un-competitive Correct MC4caf_cfd3
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]).
competitive Incorrect non-competitive Incorrect ortho-competitive Incorrect proto-competitive Incorrect un-competitive Correct MC64d5_9d15
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 | 1.2 |
| 0.002 | 7.7 | 2.4 |
| 0.005 | 18.2 | 5.5 |
| 0.010 | 33.4 | 10.0 |
| 0.020 | 57.2 | 17.2 |
| 0.050 | 100.0 | 30.0 |
| 0.100 | 133.4 | 40.0 |
| 0.200 | 160.0 | 48.0 |
| 0.500 | 181.9 | 54.6 |
| 1.000 | 190.5 | 57.2 |
| 2.000 | 195.2 | 58.6 |
| 5.000 | 198.1 | 59.5 |
| 10.000 | 199.1 | 59.8 |
| 20.000 | 199.6 | 59.9 |
| 50.000 | 199.9 | 60.0 |
| 100.000 | 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 self-competitive Incorrect un-competitive Incorrect MC8121_df44
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 | 1.0 |
| 0.002 | 50.0 | 2.0 |
| 0.005 | 71.5 | 4.8 |
| 0.010 | 83.4 | 9.1 |
| 0.020 | 91.0 | 16.7 |
| 0.050 | 96.2 | 33.4 |
| 0.100 | 98.1 | 50.0 |
| 0.200 | 99.1 | 66.7 |
| 0.500 | 99.7 | 83.4 |
| 1.000 | 99.9 | 91.0 |
| 2.000 | 100.0 | 95.3 |
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 mega-competitive Incorrect non-competitive Incorrect quasi-competitive Incorrect un-competitive Incorrect MC061e_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 | 6.7 | 0.1 |
| 0.002 | 11.5 | 0.1 |
| 0.005 | 20.0 | 0.1 |
| 0.010 | 26.7 | 0.1 |
| 0.020 | 32.0 | 0.1 |
| 0.050 | 36.4 | 0.2 |
| 0.100 | 38.1 | 0.4 |
| 0.200 | 39.1 | 0.8 |
| 0.500 | 39.7 | 2.0 |
| 1.000 | 39.9 | 3.7 |
| 2.000 | 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 inter-competitive Incorrect non-competitive Incorrect pseudo-competitive Incorrect un-competitive Incorrect MC607c_58ac
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 over-competitive Incorrect para-competitive Incorrect un-competitive Correct MC7b8c_a6d9
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 | 0.1 |
| 0.002 | 28.6 | 0.1 |
| 0.005 | 50.0 | 0.1 |
| 0.010 | 66.7 | 0.2 |
| 0.020 | 80.0 | 0.4 |
| 0.050 | 91.0 | 1.0 |
| 0.100 | 95.3 | 2.0 |
| 0.200 | 97.6 | 3.9 |
| 0.500 | 99.1 | 9.1 |
| 1.000 | 99.6 | 16.7 |
| 2.000 | 99.8 | 28.6 |
| 5.000 | 100.0 | 50.0 |
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 mega-competitive Incorrect non-competitive Incorrect self-competitive Incorrect un-competitive Incorrect MC288c_d7fb
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 hyper-competitive Incorrect non-competitive Correct para-competitive Incorrect un-competitive Incorrect MCcfaf_3e92
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 non-competitive Correct post-competitive Incorrect pre-competitive Incorrect un-competitive Incorrect MCa447_e71a
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 extra-competitive Incorrect non-competitive Incorrect proto-competitive Incorrect un-competitive Correct MC52d0_8fb6
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 | 0.2 |
| 0.005 | 20.0 | 0.5 |
| 0.010 | 33.4 | 1.0 |
| 0.020 | 50.0 | 2.0 |
| 0.050 | 71.5 | 4.8 |
| 0.100 | 83.4 | 9.1 |
| 0.200 | 91.0 | 16.7 |
| 0.500 | 96.2 | 33.4 |
| 1.000 | 98.1 | 50.0 |
| 2.000 | 99.1 | 66.7 |
| 5.000 | 99.7 | 83.4 |
| 10.000 | 99.9 | 91.0 |
| 20.000 | 100.0 | 95.3 |
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]).
anti-competitive Incorrect competitive Correct inter-competitive Incorrect non-competitive Incorrect un-competitive Incorrect MC283d_e57b
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 | 2.9 |
| 0.002 | 9.1 | 5.5 |
| 0.005 | 20.0 | 12.0 |
| 0.010 | 33.4 | 20.0 |
| 0.020 | 50.0 | 30.0 |
| 0.050 | 71.5 | 42.9 |
| 0.100 | 83.4 | 50.0 |
| 0.200 | 91.0 | 54.6 |
| 0.500 | 96.2 | 57.7 |
| 1.000 | 98.1 | 58.9 |
| 2.000 | 99.1 | 59.5 |
| 5.000 | 99.7 | 59.8 |
| 10.000 | 99.9 | 59.9 |
| 20.000 | 100.0 | 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 iso-competitive Incorrect non-competitive Correct over-competitive Incorrect un-competitive Incorrect MC2f03_9dd6
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 | 1.2 |
| 0.002 | 3.9 | 2.4 |
| 0.005 | 9.1 | 5.5 |
| 0.010 | 16.7 | 10.0 |
| 0.020 | 28.6 | 17.2 |
| 0.050 | 50.0 | 30.0 |
| 0.100 | 66.7 | 40.0 |
| 0.200 | 80.0 | 48.0 |
| 0.500 | 91.0 | 54.6 |
| 1.000 | 95.3 | 57.2 |
| 2.000 | 97.6 | 58.6 |
| 5.000 | 99.1 | 59.5 |
| 10.000 | 99.6 | 59.8 |
| 20.000 | 99.8 | 59.9 |
| 50.000 | 100.0 | 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 non-competitive Correct supra-competitive Incorrect un-competitive Incorrect MCea46_d7ef
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 hyper-competitive Incorrect non-competitive Correct oligo-competitive Incorrect un-competitive Incorrect MC2910_5408
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 | 6.7 |
| 0.002 | 100.0 | 10.0 |
| 0.005 | 142.9 | 14.3 |
| 0.010 | 166.7 | 16.7 |
| 0.020 | 181.9 | 18.2 |
| 0.050 | 192.4 | 19.3 |
| 0.100 | 196.1 | 19.7 |
| 0.200 | 198.1 | 19.9 |
| 0.500 | 199.3 | 20.0 |
| 1.000 | 199.7 | 20.0 |
| 2.000 | 199.9 | 20.0 |
| 5.000 | 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]).
anti-competitive Incorrect competitive Incorrect non-competitive Correct proto-competitive Incorrect un-competitive Incorrect MCcf9f_0b84
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 hypo-competitive Incorrect non-competitive Incorrect para-competitive Incorrect un-competitive Correct MCea20_b8c3
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 dis-competitive Incorrect non-competitive Incorrect pre-competitive Incorrect un-competitive Correct MCb0f6_09b2
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 | 0.1 |
| 0.002 | 20.0 | 0.1 |
| 0.005 | 40.0 | 0.1 |
| 0.010 | 60.0 | 0.2 |
| 0.020 | 80.0 | 0.3 |
| 0.050 | 100.0 | 0.6 |
| 0.100 | 109.1 | 1.2 |
| 0.200 | 114.3 | 2.4 |
| 0.500 | 117.7 | 5.8 |
| 1.000 | 118.9 | 11.0 |
| 2.000 | 119.5 | 20.0 |
| 5.000 | 119.8 | 40.0 |
| 10.000 | 119.9 | 60.0 |
| 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]).
auto-competitive Incorrect competitive Correct mega-competitive Incorrect non-competitive Incorrect un-competitive Incorrect MCf162_6b85
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]).
anti-competitive Incorrect competitive Incorrect hetero-competitive Incorrect non-competitive Incorrect un-competitive Correct MC67ab_ed69
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 | 2.0 |
| 0.002 | 18.2 | 4.0 |
| 0.005 | 40.0 | 9.6 |
| 0.010 | 66.7 | 18.2 |
| 0.020 | 100.0 | 33.4 |
| 0.050 | 142.9 | 66.7 |
| 0.100 | 166.7 | 100.0 |
| 0.200 | 181.9 | 133.4 |
| 0.500 | 192.4 | 166.7 |
| 1.000 | 196.1 | 181.9 |
| 2.000 | 198.1 | 190.5 |
| 5.000 | 199.3 | 196.1 |
| 10.000 | 199.7 | 198.1 |
| 20.000 | 199.9 | 199.1 |
| 50.000 | 200.0 | 199.7 |
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 intra-competitive Incorrect non-competitive Incorrect quasi-competitive Incorrect un-competitive Incorrect MC8136_d4c2
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 idio-competitive Incorrect non-competitive Incorrect pre-competitive Incorrect un-competitive Incorrect MC1f55_a95d
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 non-competitive Incorrect pseudo-competitive Incorrect un-competitive Correct MC924c_8187
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 | 0.4 |
| 0.002 | 51.5 | 0.8 |
| 0.005 | 90.0 | 1.8 |
| 0.010 | 120.1 | 3.6 |
| 0.020 | 144.0 | 7.0 |
| 0.050 | 163.7 | 16.4 |
| 0.100 | 171.5 | 30.0 |
| 0.200 | 175.7 | 51.5 |
| 0.500 | 178.3 | 90.0 |
| 1.000 | 179.2 | 120.0 |
| 2.000 | 179.6 | 144.0 |
| 5.000 | 179.9 | 163.7 |
| 10.000 | 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 oligo-competitive Incorrect supra-competitive Incorrect un-competitive Incorrect MCb7cb_35bb
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 homo-competitive Incorrect non-competitive Incorrect quasi-competitive Incorrect un-competitive Correct MCa87a_28bd
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 homo-competitive Incorrect non-competitive Incorrect ortho-competitive Incorrect un-competitive Correct MC313a_3725
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 non-competitive Incorrect poly-competitive Incorrect pre-competitive Incorrect un-competitive Correct MC4163_05c8
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 | 26.7 |
| 0.002 | 70.0 | 40.0 |
| 0.005 | 100.1 | 57.2 |
| 0.010 | 116.7 | 66.7 |
| 0.020 | 127.3 | 72.8 |
| 0.050 | 134.7 | 77.0 |
| 0.100 | 137.3 | 78.5 |
| 0.200 | 138.7 | 79.3 |
| 0.500 | 139.5 | 79.7 |
| 1.000 | 139.8 | 79.9 |
| 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 Correct post-competitive Incorrect semi-competitive Incorrect un-competitive Incorrect MC1de0_8fec
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 | 30.0 |
| 0.002 | 57.2 | 51.5 |
| 0.005 | 100.0 | 90.0 |
| 0.010 | 133.4 | 120.1 |
| 0.020 | 160.0 | 144.0 |
| 0.050 | 181.9 | 163.7 |
| 0.100 | 190.5 | 171.5 |
| 0.200 | 195.2 | 175.7 |
| 0.500 | 198.1 | 178.3 |
| 1.000 | 199.1 | 179.2 |
| 2.000 | 199.6 | 179.6 |
| 5.000 | 199.9 | 179.9 |
| 10.000 | 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 extra-competitive Incorrect non-competitive Correct poly-competitive Incorrect un-competitive Incorrect MC793b_186a
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]).
competitive Incorrect non-competitive Incorrect poly-competitive Incorrect self-competitive Incorrect un-competitive Correct MC6feb_1962
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 | 22.9 | 17.2 |
| 0.005 | 40.0 | 30.0 |
| 0.010 | 53.4 | 40.0 |
| 0.020 | 64.0 | 48.0 |
| 0.050 | 72.8 | 54.6 |
| 0.100 | 76.2 | 57.2 |
| 0.200 | 78.1 | 58.6 |
| 0.500 | 79.3 | 59.5 |
| 1.000 | 79.7 | 59.8 |
| 2.000 | 79.9 | 59.9 |
| 5.000 | 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 inter-competitive Incorrect mis-competitive Incorrect non-competitive Correct un-competitive Incorrect MC38cc_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 | 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]).
competitive Incorrect non-competitive Incorrect over-competitive Incorrect super-competitive Incorrect un-competitive Correct MC45f5_cd94
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 non-competitive Incorrect poly-competitive Incorrect super-competitive Incorrect un-competitive Correct MC0ae2_04cc
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 non-competitive Incorrect pre-competitive Incorrect self-competitive Incorrect un-competitive Correct MC912d_bd3e
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 hypo-competitive Incorrect iso-competitive Incorrect non-competitive Incorrect un-competitive Correct MC510e_1c75
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 | 5.8 |
| 0.002 | 60.0 | 11.0 |
| 0.005 | 85.8 | 24.0 |
| 0.010 | 100.0 | 40.0 |
| 0.020 | 109.1 | 60.0 |
| 0.050 | 115.4 | 85.8 |
| 0.100 | 117.7 | 100.0 |
| 0.200 | 118.9 | 109.1 |
| 0.500 | 119.6 | 115.4 |
| 1.000 | 119.8 | 117.7 |
| 2.000 | 119.9 | 118.9 |
| 5.000 | 120.0 | 119.6 |
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 non-competitive Incorrect pseudo-competitive Incorrect super-competitive Incorrect un-competitive Incorrect MC2160_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 | 18.2 | 1.0 |
| 0.002 | 33.4 | 2.0 |
| 0.005 | 66.7 | 4.9 |
| 0.010 | 100.0 | 9.6 |
| 0.020 | 133.4 | 18.2 |
| 0.050 | 166.7 | 40.0 |
| 0.100 | 181.9 | 66.7 |
| 0.200 | 190.5 | 100.0 |
| 0.500 | 196.1 | 142.9 |
| 1.000 | 198.1 | 166.7 |
| 2.000 | 199.1 | 181.9 |
| 5.000 | 199.7 | 192.4 |
| 10.000 | 199.9 | 196.1 |
| 20.000 | 200.0 | 198.1 |
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 proto-competitive Incorrect un-competitive Incorrect MC030a_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 | 2.8 | 0.1 |
| 0.002 | 5.4 | 0.2 |
| 0.005 | 12.8 | 0.4 |
| 0.010 | 23.4 | 0.7 |
| 0.020 | 40.0 | 1.4 |
| 0.050 | 70.0 | 3.5 |
| 0.100 | 93.4 | 6.7 |
| 0.200 | 112.0 | 12.8 |
| 0.500 | 127.3 | 28.0 |
| 1.000 | 133.4 | 46.7 |
| 2.000 | 136.6 | 70.0 |
| 5.000 | 138.7 | 100.0 |
| 10.000 | 139.4 | 116.7 |
| 20.000 | 139.7 | 127.3 |
| 50.000 | 139.9 | 134.7 |
| 100.000 | 140.0 | 137.3 |
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 dis-competitive Incorrect non-competitive Incorrect para-competitive Incorrect un-competitive Incorrect MCa9e6_a69e
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 | 0.7 |
| 0.002 | 70.0 | 1.4 |
| 0.005 | 100.1 | 3.5 |
| 0.010 | 116.7 | 6.7 |
| 0.020 | 127.3 | 12.8 |
| 0.050 | 134.7 | 28.0 |
| 0.100 | 137.3 | 46.7 |
| 0.200 | 138.7 | 70.0 |
| 0.500 | 139.5 | 100.0 |
| 1.000 | 139.8 | 116.7 |
| 2.000 | 139.9 | 127.3 |
| 5.000 | 140.0 | 134.7 |
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 omni-competitive Incorrect semi-competitive Incorrect un-competitive Incorrect MC67d7_60ca
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 | 0.1 |
| 0.002 | 6.2 | 0.1 |
| 0.005 | 14.6 | 0.1 |
| 0.010 | 26.7 | 0.2 |
| 0.020 | 45.8 | 0.4 |
| 0.050 | 80.0 | 0.8 |
| 0.100 | 106.7 | 1.6 |
| 0.200 | 128.0 | 3.2 |
| 0.500 | 145.5 | 7.7 |
| 1.000 | 152.4 | 14.6 |
| 2.000 | 156.1 | 26.7 |
| 5.000 | 158.5 | 53.4 |
| 10.000 | 159.3 | 80.0 |
| 20.000 | 159.7 | 106.7 |
| 50.000 | 159.9 | 133.4 |
| 100.000 | 160.0 | 145.5 |
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 hypo-competitive Incorrect non-competitive Incorrect omni-competitive Incorrect un-competitive Incorrect MCaad8_5b1b
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 | 0.2 |
| 0.002 | 22.9 | 0.4 |
| 0.005 | 40.0 | 0.8 |
| 0.010 | 53.4 | 1.6 |
| 0.020 | 64.0 | 3.1 |
| 0.050 | 72.8 | 7.3 |
| 0.100 | 76.2 | 13.4 |
| 0.200 | 78.1 | 22.9 |
| 0.500 | 79.3 | 40.0 |
| 1.000 | 79.7 | 53.4 |
| 2.000 | 79.9 | 64.0 |
| 5.000 | 80.0 | 72.8 |
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 quasi-competitive Incorrect un-competitive Incorrect MC4894_ed1d
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 | 0.2 |
| 0.002 | 7.3 | 0.4 |
| 0.005 | 16.0 | 0.8 |
| 0.010 | 26.7 | 1.6 |
| 0.020 | 40.0 | 3.1 |
| 0.050 | 57.2 | 7.3 |
| 0.100 | 66.7 | 13.4 |
| 0.200 | 72.8 | 22.9 |
| 0.500 | 77.0 | 40.0 |
| 1.000 | 78.5 | 53.4 |
| 2.000 | 79.3 | 64.0 |
| 5.000 | 79.7 | 72.8 |
| 10.000 | 79.9 | 76.2 |
| 20.000 | 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 mis-competitive Incorrect non-competitive Incorrect ortho-competitive Incorrect un-competitive Incorrect MCd506_79a1
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 | 0.6 |
| 0.002 | 34.3 | 1.2 |
| 0.005 | 60.0 | 3.0 |
| 0.010 | 80.0 | 5.8 |
| 0.020 | 96.0 | 11.0 |
| 0.050 | 109.1 | 24.0 |
| 0.100 | 114.3 | 40.0 |
| 0.200 | 117.1 | 60.0 |
| 0.500 | 118.9 | 85.8 |
| 1.000 | 119.5 | 100.0 |
| 2.000 | 119.8 | 109.1 |
| 5.000 | 119.9 | 115.4 |
| 10.000 | 120.0 | 117.7 |
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 intra-competitive Incorrect non-competitive Incorrect proto-competitive Incorrect un-competitive Incorrect MCad21_7ce0
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 | 0.4 |
| 0.002 | 45.8 | 0.7 |
| 0.005 | 80.0 | 1.6 |
| 0.010 | 106.7 | 3.2 |
| 0.020 | 128.0 | 6.2 |
| 0.050 | 145.5 | 14.6 |
| 0.100 | 152.4 | 26.7 |
| 0.200 | 156.1 | 45.8 |
| 0.500 | 158.5 | 80.0 |
| 1.000 | 159.3 | 106.7 |
| 2.000 | 159.7 | 128.0 |
| 5.000 | 159.9 | 145.5 |
| 10.000 | 160.0 | 152.4 |
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 hetero-competitive Incorrect non-competitive Incorrect pseudo-competitive Incorrect un-competitive Incorrect MCfc38_f06f
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 | 3.9 |
| 0.002 | 12.8 | 7.3 |
| 0.005 | 28.0 | 16.0 |
| 0.010 | 46.7 | 26.7 |
| 0.020 | 70.0 | 40.0 |
| 0.050 | 100.0 | 57.2 |
| 0.100 | 116.7 | 66.7 |
| 0.200 | 127.3 | 72.8 |
| 0.500 | 134.7 | 77.0 |
| 1.000 | 137.3 | 78.5 |
| 2.000 | 138.7 | 79.3 |
| 5.000 | 139.5 | 79.7 |
| 10.000 | 139.8 | 79.9 |
| 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 intra-competitive Incorrect non-competitive Correct ortho-competitive Incorrect un-competitive Incorrect MC8df8_e691
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 | 1.9 |
| 0.002 | 33.4 | 3.4 |
| 0.005 | 66.7 | 6.7 |
| 0.010 | 100.0 | 10.0 |
| 0.020 | 133.4 | 13.4 |
| 0.050 | 166.7 | 16.7 |
| 0.100 | 181.9 | 18.2 |
| 0.200 | 190.5 | 19.1 |
| 0.500 | 196.1 | 19.7 |
| 1.000 | 198.1 | 19.9 |
| 2.000 | 199.1 | 20.0 |
| 5.000 | 199.7 | 20.0 |
| 10.000 | 199.9 | 20.0 |
| 20.000 | 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 hypo-competitive Incorrect non-competitive Correct supra-competitive Incorrect un-competitive Incorrect MCffd7_ce91
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 | 0.1 |
| 0.002 | 4.7 | 0.1 |
| 0.005 | 11.0 | 0.2 |
| 0.010 | 20.0 | 0.3 |
| 0.020 | 34.3 | 0.5 |
| 0.050 | 60.0 | 1.2 |
| 0.100 | 80.0 | 2.4 |
| 0.200 | 96.0 | 4.7 |
| 0.500 | 109.1 | 11.0 |
| 1.000 | 114.3 | 20.0 |
| 2.000 | 117.1 | 34.3 |
| 5.000 | 118.9 | 60.0 |
| 10.000 | 119.5 | 80.0 |
| 20.000 | 119.8 | 96.0 |
| 50.000 | 119.9 | 109.1 |
| 100.000 | 120.0 | 114.3 |
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 omni-competitive Incorrect para-competitive Incorrect un-competitive Incorrect MCdbc1_ee3d
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 hetero-competitive Incorrect non-competitive Incorrect un-competitive Correct MC4a1f_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 | 16.4 | 0.9 |
| 0.002 | 30.0 | 1.8 |
| 0.005 | 60.1 | 4.4 |
| 0.010 | 90.0 | 8.6 |
| 0.020 | 120.1 | 16.4 |
| 0.050 | 150.0 | 36.0 |
| 0.100 | 163.7 | 60.0 |
| 0.200 | 171.5 | 90.0 |
| 0.500 | 176.5 | 128.6 |
| 1.000 | 178.3 | 150.0 |
| 2.000 | 179.2 | 163.7 |
| 5.000 | 179.7 | 173.1 |
| 10.000 | 179.9 | 176.5 |
| 20.000 | 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 eco-competitive Incorrect homo-competitive Incorrect non-competitive Incorrect un-competitive Incorrect MCdd33_d00a
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 non-competitive Incorrect proto-competitive Incorrect quasi-competitive Incorrect un-competitive Correct MCc22c_5255
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 | 0.9 |
| 0.002 | 7.0 | 1.8 |
| 0.005 | 16.4 | 4.4 |
| 0.010 | 30.0 | 8.6 |
| 0.020 | 51.5 | 16.4 |
| 0.050 | 90.0 | 36.0 |
| 0.100 | 120.0 | 60.0 |
| 0.200 | 144.0 | 90.0 |
| 0.500 | 163.7 | 128.6 |
| 1.000 | 171.5 | 150.0 |
| 2.000 | 175.7 | 163.7 |
| 5.000 | 178.3 | 173.1 |
| 10.000 | 179.2 | 176.5 |
| 20.000 | 179.6 | 178.3 |
| 50.000 | 179.9 | 179.3 |
| 100.000 | 180.0 | 179.7 |
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 hetero-competitive Incorrect non-competitive Incorrect pre-competitive Incorrect un-competitive Incorrect MCc00a_3881
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 | 0.1 |
| 0.002 | 11.0 | 0.1 |
| 0.005 | 24.0 | 0.2 |
| 0.010 | 40.0 | 0.3 |
| 0.020 | 60.0 | 0.5 |
| 0.050 | 85.8 | 1.2 |
| 0.100 | 100.0 | 2.4 |
| 0.200 | 109.1 | 4.7 |
| 0.500 | 115.4 | 11.0 |
| 1.000 | 117.7 | 20.0 |
| 2.000 | 118.9 | 34.3 |
| 5.000 | 119.6 | 60.0 |
| 10.000 | 119.8 | 80.0 |
| 20.000 | 119.9 | 96.0 |
| 50.000 | 120.0 | 109.1 |
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 mega-competitive Incorrect non-competitive Incorrect super-competitive Incorrect un-competitive Incorrect MCb292_b585
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 dis-competitive Incorrect extra-competitive Incorrect non-competitive Correct un-competitive Incorrect MC19b0_b8d9
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 | 0.3 |
| 0.002 | 5.5 | 0.6 |
| 0.005 | 12.0 | 1.5 |
| 0.010 | 20.0 | 2.9 |
| 0.020 | 30.0 | 5.5 |
| 0.050 | 42.9 | 12.0 |
| 0.100 | 50.0 | 20.0 |
| 0.200 | 54.6 | 30.0 |
| 0.500 | 57.7 | 42.9 |
| 1.000 | 58.9 | 50.0 |
| 2.000 | 59.5 | 54.6 |
| 5.000 | 59.8 | 57.7 |
| 10.000 | 59.9 | 58.9 |
| 20.000 | 60.0 | 59.5 |
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]).
anti-competitive Incorrect competitive Correct mis-competitive Incorrect non-competitive Incorrect un-competitive Incorrect MC8424_9e86
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 | 9.1 |
| 0.002 | 26.7 | 16.7 |
| 0.005 | 53.4 | 33.4 |
| 0.010 | 80.0 | 50.0 |
| 0.020 | 106.7 | 66.7 |
| 0.050 | 133.4 | 83.4 |
| 0.100 | 145.5 | 91.0 |
| 0.200 | 152.4 | 95.3 |
| 0.500 | 156.9 | 98.1 |
| 1.000 | 158.5 | 99.1 |
| 2.000 | 159.3 | 99.6 |
| 5.000 | 159.7 | 99.9 |
| 10.000 | 159.9 | 100.0 |
| 20.000 | 160.0 | 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]).
anti-competitive Incorrect competitive Incorrect non-competitive Correct over-competitive Incorrect un-competitive Incorrect MC3a78_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 | 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 dis-competitive Incorrect non-competitive Incorrect para-competitive Incorrect un-competitive Correct MCe771_8846
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 | 2.8 |
| 0.002 | 7.0 | 5.4 |
| 0.005 | 16.4 | 12.8 |
| 0.010 | 30.0 | 23.4 |
| 0.020 | 51.5 | 40.0 |
| 0.050 | 90.0 | 70.0 |
| 0.100 | 120.0 | 93.4 |
| 0.200 | 144.0 | 112.0 |
| 0.500 | 163.7 | 127.3 |
| 1.000 | 171.5 | 133.4 |
| 2.000 | 175.7 | 136.6 |
| 5.000 | 178.3 | 138.7 |
| 10.000 | 179.2 | 139.4 |
| 20.000 | 179.6 | 139.7 |
| 50.000 | 179.9 | 139.9 |
| 100.000 | 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 non-competitive Correct oligo-competitive Incorrect super-competitive Incorrect un-competitive Incorrect MCf912_b829
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 | 2.0 |
| 0.002 | 16.4 | 3.7 |
| 0.005 | 36.0 | 8.0 |
| 0.010 | 60.1 | 13.4 |
| 0.020 | 90.0 | 20.0 |
| 0.050 | 128.6 | 28.6 |
| 0.100 | 150.0 | 33.4 |
| 0.200 | 163.7 | 36.4 |
| 0.500 | 173.1 | 38.5 |
| 1.000 | 176.5 | 39.3 |
| 2.000 | 178.3 | 39.7 |
| 5.000 | 179.3 | 39.9 |
| 10.000 | 179.7 | 40.0 |
| 20.000 | 179.9 | 40.0 |
| 50.000 | 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 non-competitive Correct pre-competitive Incorrect super-competitive Incorrect un-competitive Incorrect MC5cbf_58ac
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 non-competitive Incorrect over-competitive Incorrect para-competitive Incorrect un-competitive Correct MC9268_719c
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]).
auto-competitive Incorrect competitive Incorrect extra-competitive Incorrect non-competitive Incorrect un-competitive Correct MCb180_f0ab
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 | 2.9 |
| 0.002 | 11.0 | 5.5 |
| 0.005 | 24.0 | 12.0 |
| 0.010 | 40.0 | 20.0 |
| 0.020 | 60.0 | 30.0 |
| 0.050 | 85.8 | 42.9 |
| 0.100 | 100.0 | 50.0 |
| 0.200 | 109.1 | 54.6 |
| 0.500 | 115.4 | 57.7 |
| 1.000 | 117.7 | 58.9 |
| 2.000 | 118.9 | 59.5 |
| 5.000 | 119.6 | 59.8 |
| 10.000 | 119.8 | 59.9 |
| 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 hetero-competitive Incorrect iso-competitive Incorrect non-competitive Correct un-competitive Incorrect MCfa90_9417
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 | 0.8 |
| 0.002 | 3.1 | 1.6 |
| 0.005 | 7.3 | 3.7 |
| 0.010 | 13.4 | 6.7 |
| 0.020 | 22.9 | 11.5 |
| 0.050 | 40.0 | 20.0 |
| 0.100 | 53.4 | 26.7 |
| 0.200 | 64.0 | 32.0 |
| 0.500 | 72.8 | 36.4 |
| 1.000 | 76.2 | 38.1 |
| 2.000 | 78.1 | 39.1 |
| 5.000 | 79.3 | 39.7 |
| 10.000 | 79.7 | 39.9 |
| 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 extra-competitive Incorrect non-competitive Correct super-competitive Incorrect un-competitive Incorrect MC831f_09b2
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]).
auto-competitive Incorrect competitive Incorrect mega-competitive Incorrect non-competitive Incorrect un-competitive Correct MC2176_e8a4
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 | 5.5 |
| 0.002 | 16.7 | 10.0 |
| 0.005 | 33.4 | 20.0 |
| 0.010 | 50.0 | 30.0 |
| 0.020 | 66.7 | 40.0 |
| 0.050 | 83.4 | 50.0 |
| 0.100 | 91.0 | 54.6 |
| 0.200 | 95.3 | 57.2 |
| 0.500 | 98.1 | 58.9 |
| 1.000 | 99.1 | 59.5 |
| 2.000 | 99.6 | 59.8 |
| 5.000 | 99.9 | 59.9 |
| 10.000 | 100.0 | 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 eco-competitive Incorrect non-competitive Correct supra-competitive Incorrect un-competitive Incorrect MC456d_ee38
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 | 0.4 |
| 0.002 | 57.2 | 0.8 |
| 0.005 | 100.0 | 2.0 |
| 0.010 | 133.4 | 4.0 |
| 0.020 | 160.0 | 7.7 |
| 0.050 | 181.9 | 18.2 |
| 0.100 | 190.5 | 33.4 |
| 0.200 | 195.2 | 57.2 |
| 0.500 | 198.1 | 100.0 |
| 1.000 | 199.1 | 133.4 |
| 2.000 | 199.6 | 160.0 |
| 5.000 | 199.9 | 181.9 |
| 10.000 | 200.0 | 190.5 |
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 semi-competitive Incorrect un-competitive Incorrect MC5013_2ea5
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 | 0.2 |
| 0.010 | 30.0 | 0.3 |
| 0.020 | 40.0 | 0.6 |
| 0.050 | 50.0 | 1.5 |
| 0.100 | 54.6 | 2.9 |
| 0.200 | 57.2 | 5.5 |
| 0.500 | 58.9 | 12.0 |
| 1.000 | 59.5 | 20.0 |
| 2.000 | 59.8 | 30.0 |
| 5.000 | 59.9 | 42.9 |
| 10.000 | 60.0 | 50.0 |
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 hypo-competitive Incorrect intra-competitive Incorrect non-competitive Incorrect un-competitive Incorrect MC891f_84c0
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 homo-competitive Incorrect non-competitive Incorrect over-competitive Incorrect un-competitive Correct MC9c76_10b6
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 | 2.0 |
| 0.002 | 5.5 | 3.7 |
| 0.005 | 12.0 | 8.0 |
| 0.010 | 20.0 | 13.4 |
| 0.020 | 30.0 | 20.0 |
| 0.050 | 42.9 | 28.6 |
| 0.100 | 50.0 | 33.4 |
| 0.200 | 54.6 | 36.4 |
| 0.500 | 57.7 | 38.5 |
| 1.000 | 58.9 | 39.3 |
| 2.000 | 59.5 | 39.7 |
| 5.000 | 59.8 | 39.9 |
| 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 contra-competitive Incorrect non-competitive Correct pre-competitive Incorrect un-competitive Incorrect MC1d5c_10b6
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 | 0.2 |
| 0.005 | 8.0 | 0.4 |
| 0.010 | 13.4 | 0.8 |
| 0.020 | 20.0 | 1.6 |
| 0.050 | 28.6 | 3.7 |
| 0.100 | 33.4 | 6.7 |
| 0.200 | 36.4 | 11.5 |
| 0.500 | 38.5 | 20.0 |
| 1.000 | 39.3 | 26.7 |
| 2.000 | 39.7 | 32.0 |
| 5.000 | 39.9 | 36.4 |
| 10.000 | 40.0 | 38.1 |
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 contra-competitive Incorrect non-competitive Incorrect pre-competitive Incorrect un-competitive Incorrect MC414b_bc1f
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 dis-competitive Incorrect non-competitive Incorrect quasi-competitive Incorrect un-competitive Incorrect MC0a11_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 | 8.6 | 0.1 |
| 0.002 | 16.4 | 0.1 |
| 0.005 | 36.0 | 0.1 |
| 0.010 | 60.1 | 0.1 |
| 0.020 | 90.0 | 0.2 |
| 0.050 | 128.6 | 0.5 |
| 0.100 | 150.0 | 0.9 |
| 0.200 | 163.7 | 1.8 |
| 0.500 | 173.1 | 4.4 |
| 1.000 | 176.5 | 8.6 |
| 2.000 | 178.3 | 16.4 |
| 5.000 | 179.3 | 36.0 |
| 10.000 | 179.7 | 60.0 |
| 20.000 | 179.9 | 90.0 |
| 50.000 | 180.0 | 128.6 |
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]).
auto-competitive Incorrect competitive Correct non-competitive Incorrect semi-competitive Incorrect un-competitive Incorrect MC42fe_8187
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 non-competitive Incorrect oligo-competitive Incorrect supra-competitive Incorrect un-competitive Correct MC6561_9dd6
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 extra-competitive Incorrect non-competitive Incorrect supra-competitive Incorrect un-competitive Correct MC594c_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 | 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 inter-competitive Incorrect non-competitive Incorrect self-competitive Incorrect un-competitive Correct MCae47_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 | 3.7 | 2.0 |
| 0.002 | 6.7 | 3.7 |
| 0.005 | 13.4 | 8.0 |
| 0.010 | 20.0 | 13.4 |
| 0.020 | 26.7 | 20.0 |
| 0.050 | 33.4 | 28.6 |
| 0.100 | 36.4 | 33.4 |
| 0.200 | 38.1 | 36.4 |
| 0.500 | 39.3 | 38.5 |
| 1.000 | 39.7 | 39.3 |
| 2.000 | 39.9 | 39.7 |
| 5.000 | 40.0 | 39.9 |
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]).
auto-competitive Incorrect competitive Correct non-competitive Incorrect poly-competitive Incorrect un-competitive Incorrect MCfa93_a4c7
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 mega-competitive Incorrect non-competitive Correct post-competitive Incorrect un-competitive Incorrect MCa127_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 | 33.4 | 13.4 |
| 0.002 | 50.0 | 20.0 |
| 0.005 | 71.5 | 28.6 |
| 0.010 | 83.4 | 33.4 |
| 0.020 | 91.0 | 36.4 |
| 0.050 | 96.2 | 38.5 |
| 0.100 | 98.1 | 39.3 |
| 0.200 | 99.1 | 39.7 |
| 0.500 | 99.7 | 39.9 |
| 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 non-competitive Correct pseudo-competitive Incorrect supra-competitive Incorrect un-competitive Incorrect MCac8c_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 | 9.1 | 0.1 |
| 0.002 | 16.7 | 0.2 |
| 0.005 | 33.4 | 0.5 |
| 0.010 | 50.0 | 1.0 |
| 0.020 | 66.7 | 2.0 |
| 0.050 | 83.4 | 4.8 |
| 0.100 | 91.0 | 9.1 |
| 0.200 | 95.3 | 16.7 |
| 0.500 | 98.1 | 33.4 |
| 1.000 | 99.1 | 50.0 |
| 2.000 | 99.6 | 66.7 |
| 5.000 | 99.9 | 83.4 |
| 10.000 | 100.0 | 91.0 |
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 ortho-competitive Incorrect over-competitive Incorrect un-competitive Incorrect MC8399_c0c0
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]).
anti-competitive Incorrect competitive Incorrect non-competitive Incorrect quasi-competitive Incorrect un-competitive Correct MC3848_9707
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 epi-competitive Incorrect homo-competitive Incorrect non-competitive Incorrect un-competitive Correct MC8001_df44
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]).
competitive Incorrect mega-competitive Incorrect non-competitive Incorrect quasi-competitive Incorrect un-competitive Correct MC3d5d_fb4b
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 | 11.0 |
| 0.002 | 23.4 | 20.0 |
| 0.005 | 46.7 | 40.0 |
| 0.010 | 70.0 | 60.0 |
| 0.020 | 93.4 | 80.0 |
| 0.050 | 116.7 | 100.0 |
| 0.100 | 127.3 | 109.1 |
| 0.200 | 133.4 | 114.3 |
| 0.500 | 137.3 | 117.7 |
| 1.000 | 138.7 | 118.9 |
| 2.000 | 139.4 | 119.5 |
| 5.000 | 139.8 | 119.8 |
| 10.000 | 139.9 | 119.9 |
| 20.000 | 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 oligo-competitive Incorrect proto-competitive Incorrect un-competitive Incorrect MC3e15_a9f1
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 | 0.2 |
| 0.002 | 100.0 | 0.4 |
| 0.005 | 142.9 | 1.0 |
| 0.010 | 166.7 | 2.0 |
| 0.020 | 181.9 | 4.0 |
| 0.050 | 192.4 | 9.6 |
| 0.100 | 196.1 | 18.2 |
| 0.200 | 198.1 | 33.4 |
| 0.500 | 199.3 | 66.7 |
| 1.000 | 199.7 | 100.0 |
| 2.000 | 199.9 | 133.4 |
| 5.000 | 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]).
competitive Correct non-competitive Incorrect post-competitive Incorrect supra-competitive Incorrect un-competitive Incorrect MCd9f6_6fe2
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 | 0.1 |
| 0.002 | 23.4 | 0.1 |
| 0.005 | 46.7 | 0.1 |
| 0.010 | 70.0 | 0.1 |
| 0.020 | 93.4 | 0.2 |
| 0.050 | 116.7 | 0.4 |
| 0.100 | 127.3 | 0.7 |
| 0.200 | 133.4 | 1.4 |
| 0.500 | 137.3 | 3.5 |
| 1.000 | 138.7 | 6.7 |
| 2.000 | 139.4 | 12.8 |
| 5.000 | 139.8 | 28.0 |
| 10.000 | 139.9 | 46.7 |
| 20.000 | 140.0 | 70.0 |
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 non-competitive Incorrect semi-competitive Incorrect un-competitive Incorrect MCf32e_3881
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]).
competitive Incorrect mega-competitive Incorrect non-competitive Incorrect super-competitive Incorrect un-competitive Correct MCb175_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 | 7.7 | 1.6 |
| 0.002 | 14.6 | 3.2 |
| 0.005 | 32.0 | 7.7 |
| 0.010 | 53.4 | 14.6 |
| 0.020 | 80.0 | 26.7 |
| 0.050 | 114.3 | 53.4 |
| 0.100 | 133.4 | 80.0 |
| 0.200 | 145.5 | 106.7 |
| 0.500 | 153.9 | 133.4 |
| 1.000 | 156.9 | 145.5 |
| 2.000 | 158.5 | 152.4 |
| 5.000 | 159.4 | 156.9 |
| 10.000 | 159.7 | 158.5 |
| 20.000 | 159.9 | 159.3 |
| 50.000 | 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 ultra-competitive Incorrect un-competitive Incorrect MCe037_ee38
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 | 3.7 |
| 0.002 | 30.0 | 6.7 |
| 0.005 | 60.1 | 13.4 |
| 0.010 | 90.0 | 20.0 |
| 0.020 | 120.1 | 26.7 |
| 0.050 | 150.0 | 33.4 |
| 0.100 | 163.7 | 36.4 |
| 0.200 | 171.5 | 38.1 |
| 0.500 | 176.5 | 39.3 |
| 1.000 | 178.3 | 39.7 |
| 2.000 | 179.2 | 39.9 |
| 5.000 | 179.7 | 40.0 |
| 10.000 | 179.9 | 40.0 |
| 20.000 | 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 non-competitive Correct pseudo-competitive Incorrect semi-competitive Incorrect un-competitive Incorrect MC0386_db65
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 | 20.0 |
| 0.002 | 90.0 | 30.0 |
| 0.005 | 128.6 | 42.9 |
| 0.010 | 150.0 | 50.0 |
| 0.020 | 163.7 | 54.6 |
| 0.050 | 173.1 | 57.7 |
| 0.100 | 176.5 | 58.9 |
| 0.200 | 178.3 | 59.5 |
| 0.500 | 179.3 | 59.8 |
| 1.000 | 179.7 | 59.9 |
| 2.000 | 179.9 | 60.0 |
| 5.000 | 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 iso-competitive Incorrect non-competitive Correct post-competitive Incorrect un-competitive Incorrect MCa125_8c6b
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 contra-competitive Incorrect non-competitive Incorrect para-competitive Incorrect un-competitive Incorrect MC0d0c_2ea5
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 hypo-competitive Incorrect intra-competitive Incorrect non-competitive Incorrect un-competitive Correct MCba41_84c0
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 | 10.0 |
| 0.002 | 40.0 | 17.2 |
| 0.005 | 70.0 | 30.0 |
| 0.010 | 93.4 | 40.0 |
| 0.020 | 112.0 | 48.0 |
| 0.050 | 127.3 | 54.6 |
| 0.100 | 133.4 | 57.2 |
| 0.200 | 136.6 | 58.6 |
| 0.500 | 138.7 | 59.5 |
| 1.000 | 139.4 | 59.8 |
| 2.000 | 139.7 | 59.9 |
| 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 homo-competitive Incorrect non-competitive Correct over-competitive Incorrect un-competitive Incorrect MC0ede_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 | 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 dis-competitive Incorrect non-competitive Incorrect over-competitive Incorrect un-competitive Correct MC6f4e_7e8b
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 contra-competitive Incorrect hyper-competitive Incorrect non-competitive Correct un-competitive Incorrect MC23c1_298f
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 inter-competitive Incorrect non-competitive Correct ultra-competitive Incorrect un-competitive Incorrect MC89c5_3e43
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 | 0.4 |
| 0.002 | 2.4 | 0.8 |
| 0.005 | 5.5 | 1.9 |
| 0.010 | 10.0 | 3.4 |
| 0.020 | 17.2 | 5.8 |
| 0.050 | 30.0 | 10.0 |
| 0.100 | 40.0 | 13.4 |
| 0.200 | 48.0 | 16.0 |
| 0.500 | 54.6 | 18.2 |
| 1.000 | 57.2 | 19.1 |
| 2.000 | 58.6 | 19.6 |
| 5.000 | 59.5 | 19.9 |
| 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 non-competitive Correct post-competitive Incorrect self-competitive Incorrect un-competitive Incorrect MC0849_719c
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]).
auto-competitive Incorrect competitive Incorrect extra-competitive Incorrect non-competitive Incorrect un-competitive Correct MC4edc_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 | 7.3 | 0.1 |
| 0.002 | 13.4 | 0.1 |
| 0.005 | 26.7 | 0.1 |
| 0.010 | 40.0 | 0.1 |
| 0.020 | 53.4 | 0.2 |
| 0.050 | 66.7 | 0.4 |
| 0.100 | 72.8 | 0.8 |
| 0.200 | 76.2 | 1.6 |
| 0.500 | 78.5 | 3.9 |
| 1.000 | 79.3 | 7.3 |
| 2.000 | 79.7 | 13.4 |
| 5.000 | 79.9 | 26.7 |
| 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]).
competitive Correct eco-competitive Incorrect homo-competitive Incorrect non-competitive Incorrect un-competitive Incorrect MC3b6e_5408
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 | 3.9 |
| 0.002 | 18.2 | 7.3 |
| 0.005 | 40.0 | 16.0 |
| 0.010 | 66.7 | 26.7 |
| 0.020 | 100.0 | 40.0 |
| 0.050 | 142.9 | 57.2 |
| 0.100 | 166.7 | 66.7 |
| 0.200 | 181.9 | 72.8 |
| 0.500 | 192.4 | 77.0 |
| 1.000 | 196.1 | 78.5 |
| 2.000 | 198.1 | 79.3 |
| 5.000 | 199.3 | 79.7 |
| 10.000 | 199.7 | 79.9 |
| 20.000 | 199.9 | 80.0 |
| 50.000 | 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]).
anti-competitive Incorrect competitive Incorrect non-competitive Correct proto-competitive Incorrect un-competitive Incorrect MC7008_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 | 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 hetero-competitive Incorrect non-competitive Incorrect ultra-competitive Incorrect un-competitive Correct MC6762_0866
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 contra-competitive Incorrect homo-competitive Incorrect non-competitive Incorrect un-competitive Correct MC5425_07ed
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 hetero-competitive Incorrect non-competitive Incorrect para-competitive Incorrect un-competitive Correct MCdabb_15ac
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 | 13.4 |
| 0.002 | 51.5 | 22.9 |
| 0.005 | 90.0 | 40.0 |
| 0.010 | 120.1 | 53.4 |
| 0.020 | 144.0 | 64.0 |
| 0.050 | 163.7 | 72.8 |
| 0.100 | 171.5 | 76.2 |
| 0.200 | 175.7 | 78.1 |
| 0.500 | 178.3 | 79.3 |
| 1.000 | 179.2 | 79.7 |
| 2.000 | 179.6 | 79.9 |
| 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 epi-competitive Incorrect non-competitive Correct quasi-competitive Incorrect un-competitive Incorrect MCc90d_638b
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 hypo-competitive Incorrect non-competitive Incorrect semi-competitive Incorrect un-competitive Incorrect MC02c3_bf27
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 | 0.2 |
| 0.005 | 28.6 | 0.4 |
| 0.010 | 33.4 | 0.8 |
| 0.020 | 36.4 | 1.6 |
| 0.050 | 38.5 | 3.7 |
| 0.100 | 39.3 | 6.7 |
| 0.200 | 39.7 | 11.5 |
| 0.500 | 39.9 | 20.0 |
| 1.000 | 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]).
competitive Correct epi-competitive Incorrect non-competitive Incorrect oligo-competitive Incorrect un-competitive Incorrect MC3ccb_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 | 14.6 | 0.4 |
| 0.002 | 26.7 | 0.7 |
| 0.005 | 53.4 | 1.6 |
| 0.010 | 80.0 | 3.2 |
| 0.020 | 106.7 | 6.2 |
| 0.050 | 133.4 | 14.6 |
| 0.100 | 145.5 | 26.7 |
| 0.200 | 152.4 | 45.8 |
| 0.500 | 156.9 | 80.0 |
| 1.000 | 158.5 | 106.7 |
| 2.000 | 159.3 | 128.0 |
| 5.000 | 159.7 | 145.5 |
| 10.000 | 159.9 | 152.4 |
| 20.000 | 160.0 | 156.1 |
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 poly-competitive Incorrect un-competitive Incorrect MC0cdc_3a84
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 over-competitive Incorrect pseudo-competitive Incorrect un-competitive Correct MC887a_4cfe
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 non-competitive Incorrect pseudo-competitive Incorrect un-competitive Correct MCae7d_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 | 3.2 | 1.6 |
| 0.002 | 6.2 | 3.1 |
| 0.005 | 14.6 | 7.3 |
| 0.010 | 26.7 | 13.4 |
| 0.020 | 45.8 | 22.9 |
| 0.050 | 80.0 | 40.0 |
| 0.100 | 106.7 | 53.4 |
| 0.200 | 128.0 | 64.0 |
| 0.500 | 145.5 | 72.8 |
| 1.000 | 152.4 | 76.2 |
| 2.000 | 156.1 | 78.1 |
| 5.000 | 158.5 | 79.3 |
| 10.000 | 159.3 | 79.7 |
| 20.000 | 159.7 | 79.9 |
| 50.000 | 159.9 | 80.0 |
| 100.000 | 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 contra-competitive Incorrect non-competitive Correct proto-competitive Incorrect un-competitive Incorrect MC79d9_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 | 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 inter-competitive Incorrect non-competitive Correct proto-competitive Incorrect un-competitive Incorrect MC5646_bff4
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]).
competitive Correct hyper-competitive Incorrect non-competitive Incorrect semi-competitive Incorrect un-competitive Incorrect MC9457_d4c2
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 | 1.9 |
| 0.002 | 10.0 | 3.4 |
| 0.005 | 20.0 | 6.7 |
| 0.010 | 30.0 | 10.0 |
| 0.020 | 40.0 | 13.4 |
| 0.050 | 50.0 | 16.7 |
| 0.100 | 54.6 | 18.2 |
| 0.200 | 57.2 | 19.1 |
| 0.500 | 58.9 | 19.7 |
| 1.000 | 59.5 | 19.9 |
| 2.000 | 59.8 | 20.0 |
| 5.000 | 59.9 | 20.0 |
| 10.000 | 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 idio-competitive Incorrect non-competitive Correct pre-competitive Incorrect un-competitive Incorrect MC266b_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 | 53.4 | 33.4 |
| 0.002 | 80.0 | 50.0 |
| 0.005 | 114.3 | 71.5 |
| 0.010 | 133.4 | 83.4 |
| 0.020 | 145.5 | 91.0 |
| 0.050 | 153.9 | 96.2 |
| 0.100 | 156.9 | 98.1 |
| 0.200 | 158.5 | 99.1 |
| 0.500 | 159.4 | 99.7 |
| 1.000 | 159.7 | 99.9 |
| 2.000 | 159.9 | 100.0 |
| 5.000 | 160.0 | 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 hetero-competitive Incorrect non-competitive Correct ultra-competitive Incorrect un-competitive Incorrect MCa9ca_27c9
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 | 26.7 |
| 0.002 | 80.0 | 45.8 |
| 0.005 | 114.3 | 80.0 |
| 0.010 | 133.4 | 106.7 |
| 0.020 | 145.5 | 128.0 |
| 0.050 | 153.9 | 145.5 |
| 0.100 | 156.9 | 152.4 |
| 0.200 | 158.5 | 156.1 |
| 0.500 | 159.4 | 158.5 |
| 1.000 | 159.7 | 159.3 |
| 2.000 | 159.9 | 159.7 |
| 5.000 | 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 para-competitive Incorrect ultra-competitive Incorrect un-competitive Incorrect MC04b6_0866
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 | 11.5 |
| 0.005 | 30.0 | 20.0 |
| 0.010 | 40.0 | 26.7 |
| 0.020 | 48.0 | 32.0 |
| 0.050 | 54.6 | 36.4 |
| 0.100 | 57.2 | 38.1 |
| 0.200 | 58.6 | 39.1 |
| 0.500 | 59.5 | 39.7 |
| 1.000 | 59.8 | 39.9 |
| 2.000 | 59.9 | 40.0 |
| 5.000 | 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 contra-competitive Incorrect homo-competitive Incorrect non-competitive Correct un-competitive Incorrect MCd559_130a
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 | 0.1 |
| 0.002 | 12.8 | 0.1 |
| 0.005 | 28.0 | 0.1 |
| 0.010 | 46.7 | 0.1 |
| 0.020 | 70.0 | 0.2 |
| 0.050 | 100.0 | 0.4 |
| 0.100 | 116.7 | 0.7 |
| 0.200 | 127.3 | 1.4 |
| 0.500 | 134.7 | 3.5 |
| 1.000 | 137.3 | 6.7 |
| 2.000 | 138.7 | 12.8 |
| 5.000 | 139.5 | 28.0 |
| 10.000 | 139.8 | 46.7 |
| 20.000 | 139.9 | 70.0 |
| 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 Correct epi-competitive Incorrect non-competitive Incorrect para-competitive Incorrect un-competitive Incorrect MC3494_8aab
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 | 3.7 |
| 0.002 | 20.0 | 6.7 |
| 0.005 | 40.0 | 13.4 |
| 0.010 | 60.0 | 20.0 |
| 0.020 | 80.0 | 26.7 |
| 0.050 | 100.0 | 33.4 |
| 0.100 | 109.1 | 36.4 |
| 0.200 | 114.3 | 38.1 |
| 0.500 | 117.7 | 39.3 |
| 1.000 | 118.9 | 39.7 |
| 2.000 | 119.5 | 39.9 |
| 5.000 | 119.8 | 40.0 |
| 10.000 | 119.9 | 40.0 |
| 20.000 | 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 Correct ortho-competitive Incorrect ultra-competitive Incorrect un-competitive Incorrect MC09b7_f8fa
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]).
anti-competitive Incorrect competitive Incorrect eco-competitive Incorrect non-competitive Incorrect un-competitive Correct