3657
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 6.7 | 0.1 |
| 0.0002 | 11.5 | 0.2 |
| 0.0005 | 20.0 | 0.4 |
| 0.0010 | 26.7 | 0.8 |
| 0.0020 | 32.0 | 1.6 |
| 0.0050 | 36.4 | 3.7 |
| 0.0100 | 38.1 | 6.7 |
| 0.0200 | 39.1 | 11.5 |
| 0.0500 | 39.7 | 20.0 |
| 0.1000 | 39.9 | 26.7 |
| 1.0000 | 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]).
A. competitive Correct B. hyper-competitive Incorrect C. non-competitive Incorrect D. para-competitive Incorrect E. un-competitive Incorrect MC36c6
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 26.7 | 6.7 |
| 0.0002 | 40.0 | 10.0 |
| 0.0005 | 57.2 | 14.3 |
| 0.0010 | 66.7 | 16.7 |
| 0.0020 | 72.8 | 18.2 |
| 0.0050 | 77.0 | 19.3 |
| 0.0100 | 78.5 | 19.7 |
| 0.0200 | 79.3 | 19.9 |
| 0.0500 | 79.7 | 20.0 |
| 0.1000 | 79.9 | 20.0 |
| 1.0000 | 80.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
A. competitive Incorrect B. hetero-competitive Incorrect C. non-competitive Correct D. pre-competitive Incorrect E. un-competitive Incorrect MC3746
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 5.8 | 0.3 |
| 0.0002 | 11.0 | 0.5 |
| 0.0005 | 24.0 | 1.2 |
| 0.0010 | 40.0 | 2.4 |
| 0.0020 | 60.0 | 4.7 |
| 0.0050 | 85.8 | 11.0 |
| 0.0100 | 100.0 | 20.0 |
| 0.0200 | 109.1 | 34.3 |
| 0.0500 | 115.4 | 60.0 |
| 0.1000 | 117.7 | 80.0 |
| 1.0000 | 119.8 | 114.3 |
| 10.0000 | 120.0 | 119.5 |
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]).
A. competitive Correct B. hyper-competitive Incorrect C. non-competitive Incorrect D. over-competitive Incorrect E. un-competitive Incorrect MC3939
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 60.0 | 40.0 |
| 0.0002 | 90.0 | 53.4 |
| 0.0005 | 128.6 | 66.7 |
| 0.0010 | 150.0 | 72.8 |
| 0.0020 | 163.7 | 76.2 |
| 0.0050 | 173.1 | 78.5 |
| 0.0100 | 176.5 | 79.3 |
| 0.0200 | 178.3 | 79.7 |
| 0.0500 | 179.3 | 79.9 |
| 0.1000 | 179.7 | 80.0 |
| 1.0000 | 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]).
A. competitive Incorrect B. eco-competitive Incorrect C. hyper-competitive Incorrect D. non-competitive Incorrect E. un-competitive Correct MC39b4
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 6.7 | 7.3 |
| 0.0002 | 12.8 | 13.4 |
| 0.0005 | 28.1 | 26.7 |
| 0.0010 | 46.7 | 40.0 |
| 0.0020 | 70.0 | 53.4 |
| 0.0050 | 100.1 | 66.7 |
| 0.0100 | 116.7 | 72.8 |
| 0.0200 | 127.3 | 76.2 |
| 0.0500 | 134.7 | 78.5 |
| 0.1000 | 137.3 | 79.3 |
| 1.0000 | 139.8 | 80.0 |
| 10.0000 | 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]).
A. competitive Incorrect B. mis-competitive Incorrect C. non-competitive Incorrect D. semi-competitive Incorrect E. un-competitive Correct MC3d0c
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 13.4 | 0.4 |
| 0.0002 | 22.9 | 0.8 |
| 0.0005 | 40.0 | 2.0 |
| 0.0010 | 53.4 | 3.9 |
| 0.0020 | 64.0 | 7.3 |
| 0.0050 | 72.8 | 16.0 |
| 0.0100 | 76.2 | 26.7 |
| 0.0200 | 78.1 | 40.0 |
| 0.0500 | 79.3 | 57.2 |
| 0.1000 | 79.7 | 66.7 |
| 1.0000 | 80.0 | 78.5 |
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]).
A. competitive Correct B. contra-competitive Incorrect C. hypo-competitive Incorrect D. non-competitive Incorrect E. un-competitive Incorrect MC3fda
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 2.0 | 1.0 |
| 0.0002 | 3.7 | 1.9 |
| 0.0005 | 8.0 | 4.0 |
| 0.0010 | 13.4 | 6.7 |
| 0.0020 | 20.0 | 10.0 |
| 0.0050 | 28.6 | 14.3 |
| 0.0100 | 33.4 | 16.7 |
| 0.0200 | 36.4 | 18.2 |
| 0.0500 | 38.5 | 19.3 |
| 0.1000 | 39.3 | 19.7 |
| 1.0000 | 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]).
A. competitive Incorrect B. homo-competitive Incorrect C. inter-competitive Incorrect D. non-competitive Correct E. un-competitive Incorrect MC4559
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 2.4 | 0.3 |
| 0.0002 | 4.7 | 0.5 |
| 0.0005 | 11.0 | 1.2 |
| 0.0010 | 20.0 | 2.4 |
| 0.0020 | 34.3 | 4.7 |
| 0.0050 | 60.0 | 11.0 |
| 0.0100 | 80.0 | 20.0 |
| 0.0200 | 96.0 | 34.3 |
| 0.0500 | 109.1 | 60.0 |
| 0.1000 | 114.3 | 80.0 |
| 1.0000 | 119.5 | 114.3 |
| 10.0000 | 120.0 | 119.5 |
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]).
A. competitive Correct B. intra-competitive Incorrect C. non-competitive Incorrect D. post-competitive Incorrect E. un-competitive Incorrect MC45da
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 1.2 | 1.0 |
| 0.0002 | 2.4 | 1.9 |
| 0.0005 | 5.5 | 4.0 |
| 0.0010 | 10.0 | 6.7 |
| 0.0020 | 17.2 | 10.0 |
| 0.0050 | 30.0 | 14.3 |
| 0.0100 | 40.0 | 16.7 |
| 0.0200 | 48.0 | 18.2 |
| 0.0500 | 54.6 | 19.3 |
| 0.1000 | 57.2 | 19.7 |
| 1.0000 | 59.8 | 20.0 |
| 10.0000 | 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]).
A. competitive Incorrect B. non-competitive Incorrect C. omni-competitive Incorrect D. ortho-competitive Incorrect E. un-competitive Correct MC4a73
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 14.6 | 11.0 |
| 0.0002 | 26.7 | 20.0 |
| 0.0005 | 53.4 | 40.0 |
| 0.0010 | 80.0 | 60.0 |
| 0.0020 | 106.7 | 80.0 |
| 0.0050 | 133.4 | 100.0 |
| 0.0100 | 145.5 | 109.1 |
| 0.0200 | 152.4 | 114.3 |
| 0.0500 | 156.9 | 117.7 |
| 0.1000 | 158.5 | 118.9 |
| 1.0000 | 159.9 | 119.9 |
| 10.0000 | 160.0 | 120.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
A. competitive Incorrect B. non-competitive Correct C. over-competitive Incorrect D. pseudo-competitive Incorrect E. un-competitive Incorrect MC4cb8
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 20.0 | 16.7 |
| 0.0002 | 34.3 | 28.6 |
| 0.0005 | 60.0 | 50.0 |
| 0.0010 | 80.0 | 66.7 |
| 0.0020 | 96.0 | 80.0 |
| 0.0050 | 109.1 | 91.0 |
| 0.0100 | 114.3 | 95.3 |
| 0.0200 | 117.1 | 97.6 |
| 0.0500 | 118.9 | 99.1 |
| 0.1000 | 119.5 | 99.6 |
| 1.0000 | 120.0 | 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]).
A. competitive Incorrect B. idio-competitive Incorrect C. iso-competitive Incorrect D. non-competitive Correct E. un-competitive Incorrect MC4d3b
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 7.7 | 7.3 |
| 0.0002 | 14.6 | 13.4 |
| 0.0005 | 32.0 | 26.7 |
| 0.0010 | 53.4 | 40.0 |
| 0.0020 | 80.0 | 53.4 |
| 0.0050 | 114.3 | 66.7 |
| 0.0100 | 133.4 | 72.8 |
| 0.0200 | 145.5 | 76.2 |
| 0.0500 | 153.9 | 78.5 |
| 0.1000 | 156.9 | 79.3 |
| 1.0000 | 159.7 | 80.0 |
| 10.0000 | 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]).
A. competitive Incorrect B. intra-competitive Incorrect C. non-competitive Incorrect D. over-competitive Incorrect E. un-competitive Correct MC4df8
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 2.9 | 3.7 |
| 0.0002 | 5.5 | 6.7 |
| 0.0005 | 12.0 | 13.4 |
| 0.0010 | 20.0 | 20.0 |
| 0.0020 | 30.0 | 26.7 |
| 0.0050 | 42.9 | 33.4 |
| 0.0100 | 50.0 | 36.4 |
| 0.0200 | 54.6 | 38.1 |
| 0.0500 | 57.7 | 39.3 |
| 0.1000 | 58.9 | 39.7 |
| 1.0000 | 59.9 | 40.0 |
| 10.0000 | 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]).
A. competitive Incorrect B. non-competitive Incorrect C. poly-competitive Incorrect D. ultra-competitive Incorrect E. un-competitive Correct MC4e55
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 13.4 | 6.7 |
| 0.0002 | 20.0 | 10.0 |
| 0.0005 | 28.6 | 14.3 |
| 0.0010 | 33.4 | 16.7 |
| 0.0020 | 36.4 | 18.2 |
| 0.0050 | 38.5 | 19.3 |
| 0.0100 | 39.3 | 19.7 |
| 0.0200 | 39.7 | 19.9 |
| 0.0500 | 39.9 | 20.0 |
| 0.1000 | 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]).
A. competitive Incorrect B. non-competitive Correct C. para-competitive Incorrect D. proto-competitive Incorrect E. un-competitive Incorrect MC4e82
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 40.0 | 2.4 |
| 0.0002 | 60.0 | 4.7 |
| 0.0005 | 85.8 | 11.0 |
| 0.0010 | 100.0 | 20.0 |
| 0.0020 | 109.1 | 34.3 |
| 0.0050 | 115.4 | 60.0 |
| 0.0100 | 117.7 | 80.0 |
| 0.0200 | 118.9 | 96.0 |
| 0.0500 | 119.6 | 109.1 |
| 0.1000 | 119.8 | 114.3 |
| 1.0000 | 120.0 | 119.5 |
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]).
A. competitive Correct B. non-competitive Incorrect C. oligo-competitive Incorrect D. supra-competitive Incorrect E. un-competitive Incorrect MC4ea2
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 2.8 | 0.7 |
| 0.0002 | 5.4 | 1.4 |
| 0.0005 | 12.8 | 3.5 |
| 0.0010 | 23.4 | 6.7 |
| 0.0020 | 40.0 | 12.8 |
| 0.0050 | 70.0 | 28.0 |
| 0.0100 | 93.4 | 46.7 |
| 0.0200 | 112.0 | 70.0 |
| 0.0500 | 127.3 | 100.0 |
| 0.1000 | 133.4 | 116.7 |
| 1.0000 | 139.4 | 137.3 |
| 10.0000 | 140.0 | 139.8 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
A. competitive Correct B. eco-competitive Incorrect C. non-competitive Incorrect D. ortho-competitive Incorrect E. un-competitive Incorrect MC4f58
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 9.6 | 9.1 |
| 0.0002 | 18.2 | 16.7 |
| 0.0005 | 40.0 | 33.4 |
| 0.0010 | 66.7 | 50.0 |
| 0.0020 | 100.0 | 66.7 |
| 0.0050 | 142.9 | 83.4 |
| 0.0100 | 166.7 | 91.0 |
| 0.0200 | 181.9 | 95.3 |
| 0.0500 | 192.4 | 98.1 |
| 0.1000 | 196.1 | 99.1 |
| 1.0000 | 199.7 | 100.0 |
| 10.0000 | 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]).
A. anti-competitive Incorrect B. competitive Incorrect C. homo-competitive Incorrect D. non-competitive Incorrect E. un-competitive Correct MC5050
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 53.4 | 40.0 |
| 0.0002 | 80.0 | 53.4 |
| 0.0005 | 114.3 | 66.7 |
| 0.0010 | 133.4 | 72.8 |
| 0.0020 | 145.5 | 76.2 |
| 0.0050 | 153.9 | 78.5 |
| 0.0100 | 156.9 | 79.3 |
| 0.0200 | 158.5 | 79.7 |
| 0.0500 | 159.4 | 79.9 |
| 0.1000 | 159.7 | 80.0 |
| 1.0000 | 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]).
A. competitive Incorrect B. hyper-competitive Incorrect C. non-competitive Incorrect D. proto-competitive Incorrect E. un-competitive Correct MC5068
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 12.8 | 1.9 |
| 0.0002 | 23.4 | 3.4 |
| 0.0005 | 46.7 | 6.7 |
| 0.0010 | 70.0 | 10.0 |
| 0.0020 | 93.4 | 13.4 |
| 0.0050 | 116.7 | 16.7 |
| 0.0100 | 127.3 | 18.2 |
| 0.0200 | 133.4 | 19.1 |
| 0.0500 | 137.3 | 19.7 |
| 0.1000 | 138.7 | 19.9 |
| 1.0000 | 139.9 | 20.0 |
| 10.0000 | 140.0 | 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]).
A. competitive Incorrect B. non-competitive Correct C. pseudo-competitive Incorrect D. quasi-competitive Incorrect E. un-competitive Incorrect MC5081
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 16.4 | 0.2 |
| 0.0002 | 30.0 | 0.4 |
| 0.0005 | 60.0 | 0.9 |
| 0.0010 | 90.0 | 1.8 |
| 0.0020 | 120.0 | 3.6 |
| 0.0050 | 150.0 | 8.6 |
| 0.0100 | 163.7 | 16.4 |
| 0.0200 | 171.5 | 30.0 |
| 0.0500 | 176.5 | 60.0 |
| 0.1000 | 178.3 | 90.0 |
| 1.0000 | 179.9 | 163.7 |
| 10.0000 | 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]).
A. competitive Correct B. eco-competitive Incorrect C. non-competitive Incorrect D. poly-competitive Incorrect E. un-competitive Incorrect MC51a9
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 7.7 | 0.8 |
| 0.0002 | 14.6 | 1.6 |
| 0.0005 | 32.0 | 4.0 |
| 0.0010 | 53.4 | 7.7 |
| 0.0020 | 80.0 | 14.6 |
| 0.0050 | 114.3 | 32.0 |
| 0.0100 | 133.4 | 53.4 |
| 0.0200 | 145.5 | 80.0 |
| 0.0500 | 153.9 | 114.3 |
| 0.1000 | 156.9 | 133.4 |
| 1.0000 | 159.7 | 156.9 |
| 10.0000 | 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]).
A. competitive Correct B. dis-competitive Incorrect C. non-competitive Incorrect D. pre-competitive Incorrect E. un-competitive Incorrect MC51ce
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 18.2 | 16.7 |
| 0.0002 | 33.4 | 28.6 |
| 0.0005 | 66.7 | 50.0 |
| 0.0010 | 100.0 | 66.7 |
| 0.0020 | 133.4 | 80.0 |
| 0.0050 | 166.7 | 91.0 |
| 0.0100 | 181.9 | 95.3 |
| 0.0200 | 190.5 | 97.6 |
| 0.0500 | 196.1 | 99.1 |
| 0.1000 | 198.1 | 99.6 |
| 1.0000 | 199.9 | 100.0 |
| 10.0000 | 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]).
A. competitive Incorrect B. contra-competitive Incorrect C. non-competitive Incorrect D. self-competitive Incorrect E. un-competitive Correct MC5427
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 30.0 | 1.8 |
| 0.0002 | 51.5 | 3.6 |
| 0.0005 | 90.0 | 8.6 |
| 0.0010 | 120.0 | 16.4 |
| 0.0020 | 144.0 | 30.0 |
| 0.0050 | 163.7 | 60.1 |
| 0.0100 | 171.5 | 90.0 |
| 0.0200 | 175.7 | 120.1 |
| 0.0500 | 178.3 | 150.0 |
| 0.1000 | 179.2 | 163.7 |
| 1.0000 | 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]).
A. competitive Correct B. hyper-competitive Incorrect C. mega-competitive Incorrect D. non-competitive Incorrect E. un-competitive Incorrect MC5452
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 26.7 | 0.2 |
| 0.0002 | 45.8 | 0.4 |
| 0.0005 | 80.0 | 0.8 |
| 0.0010 | 106.7 | 1.6 |
| 0.0020 | 128.0 | 3.2 |
| 0.0050 | 145.5 | 7.7 |
| 0.0100 | 152.4 | 14.6 |
| 0.0200 | 156.1 | 26.7 |
| 0.0500 | 158.5 | 53.4 |
| 0.1000 | 159.3 | 80.0 |
| 1.0000 | 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]).
A. competitive Correct B. mega-competitive Incorrect C. non-competitive Incorrect D. super-competitive Incorrect E. un-competitive Incorrect MC599c
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 6.7 | 6.7 |
| 0.0002 | 11.5 | 10.0 |
| 0.0005 | 20.0 | 14.3 |
| 0.0010 | 26.7 | 16.7 |
| 0.0020 | 32.0 | 18.2 |
| 0.0050 | 36.4 | 19.3 |
| 0.0100 | 38.1 | 19.7 |
| 0.0200 | 39.1 | 19.9 |
| 0.0500 | 39.7 | 20.0 |
| 0.1000 | 39.9 | 20.0 |
| 1.0000 | 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]).
A. anti-competitive Incorrect B. competitive Incorrect C. inter-competitive Incorrect D. non-competitive Incorrect E. un-competitive Correct MC59ef
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 40.0 | 20.0 |
| 0.0002 | 60.0 | 30.0 |
| 0.0005 | 85.8 | 42.9 |
| 0.0010 | 100.0 | 50.0 |
| 0.0020 | 109.1 | 54.6 |
| 0.0050 | 115.4 | 57.7 |
| 0.0100 | 117.7 | 58.9 |
| 0.0200 | 118.9 | 59.5 |
| 0.0500 | 119.6 | 59.8 |
| 0.1000 | 119.8 | 59.9 |
| 1.0000 | 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]).
A. competitive Incorrect B. iso-competitive Incorrect C. non-competitive Correct D. super-competitive Incorrect E. un-competitive Incorrect MC5a7c
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 4.8 | 3.7 |
| 0.0002 | 9.1 | 6.7 |
| 0.0005 | 20.0 | 13.4 |
| 0.0010 | 33.4 | 20.0 |
| 0.0020 | 50.0 | 26.7 |
| 0.0050 | 71.5 | 33.4 |
| 0.0100 | 83.4 | 36.4 |
| 0.0200 | 91.0 | 38.1 |
| 0.0500 | 96.2 | 39.3 |
| 0.1000 | 98.1 | 39.7 |
| 1.0000 | 99.9 | 40.0 |
| 10.0000 | 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]).
A. competitive Incorrect B. non-competitive Incorrect C. ortho-competitive Incorrect D. quasi-competitive Incorrect E. un-competitive Correct MC5d2c
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 46.7 | 40.0 |
| 0.0002 | 70.0 | 53.4 |
| 0.0005 | 100.1 | 66.7 |
| 0.0010 | 116.7 | 72.8 |
| 0.0020 | 127.3 | 76.2 |
| 0.0050 | 134.7 | 78.5 |
| 0.0100 | 137.3 | 79.3 |
| 0.0200 | 138.7 | 79.7 |
| 0.0500 | 139.5 | 79.9 |
| 0.1000 | 139.8 | 80.0 |
| 1.0000 | 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]).
A. competitive Incorrect B. hyper-competitive Incorrect C. non-competitive Incorrect D. para-competitive Incorrect E. un-competitive Correct MC5efc
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 7.3 | 3.7 |
| 0.0002 | 13.4 | 6.7 |
| 0.0005 | 26.7 | 13.4 |
| 0.0010 | 40.0 | 20.0 |
| 0.0020 | 53.4 | 26.7 |
| 0.0050 | 66.7 | 33.4 |
| 0.0100 | 72.8 | 36.4 |
| 0.0200 | 76.2 | 38.1 |
| 0.0500 | 78.5 | 39.3 |
| 0.1000 | 79.3 | 39.7 |
| 1.0000 | 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]).
A. auto-competitive Incorrect B. competitive Incorrect C. iso-competitive Incorrect D. non-competitive Correct E. un-competitive Incorrect MC6014
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 3.6 | 0.4 |
| 0.0002 | 7.0 | 0.8 |
| 0.0005 | 16.4 | 1.8 |
| 0.0010 | 30.0 | 3.6 |
| 0.0020 | 51.5 | 7.0 |
| 0.0050 | 90.0 | 16.4 |
| 0.0100 | 120.1 | 30.0 |
| 0.0200 | 144.0 | 51.5 |
| 0.0500 | 163.7 | 90.0 |
| 0.1000 | 171.5 | 120.0 |
| 1.0000 | 179.2 | 171.5 |
| 10.0000 | 180.0 | 179.2 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
A. competitive Correct B. contra-competitive Incorrect C. hyper-competitive Incorrect D. non-competitive Incorrect E. un-competitive Incorrect MC60c3
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 20.0 | 0.2 |
| 0.0002 | 34.3 | 0.3 |
| 0.0005 | 60.0 | 0.6 |
| 0.0010 | 80.0 | 1.2 |
| 0.0020 | 96.0 | 2.4 |
| 0.0050 | 109.1 | 5.8 |
| 0.0100 | 114.3 | 11.0 |
| 0.0200 | 117.1 | 20.0 |
| 0.0500 | 118.9 | 40.0 |
| 0.1000 | 119.5 | 60.0 |
| 1.0000 | 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]).
A. competitive Correct B. homo-competitive Incorrect C. non-competitive Incorrect D. ortho-competitive Incorrect E. un-competitive Incorrect MC62d2
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 3.6 | 3.9 |
| 0.0002 | 7.0 | 7.3 |
| 0.0005 | 16.4 | 16.0 |
| 0.0010 | 30.0 | 26.7 |
| 0.0020 | 51.5 | 40.0 |
| 0.0050 | 90.0 | 57.2 |
| 0.0100 | 120.1 | 66.7 |
| 0.0200 | 144.0 | 72.8 |
| 0.0500 | 163.7 | 77.0 |
| 0.1000 | 171.5 | 78.5 |
| 1.0000 | 179.2 | 79.9 |
| 10.0000 | 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]).
A. competitive Incorrect B. intra-competitive Incorrect C. non-competitive Incorrect D. pre-competitive Incorrect E. un-competitive Correct MC661a
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 16.7 | 4.8 |
| 0.0002 | 28.6 | 9.1 |
| 0.0005 | 50.0 | 20.0 |
| 0.0010 | 66.7 | 33.4 |
| 0.0020 | 80.0 | 50.0 |
| 0.0050 | 91.0 | 71.5 |
| 0.0100 | 95.3 | 83.4 |
| 0.0200 | 97.6 | 91.0 |
| 0.0500 | 99.1 | 96.2 |
| 0.1000 | 99.6 | 98.1 |
| 1.0000 | 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]).
A. competitive Correct B. epi-competitive Incorrect C. extra-competitive Incorrect D. non-competitive Incorrect E. un-competitive Incorrect MC68ef
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 20.0 | 20.0 |
| 0.0002 | 30.0 | 26.7 |
| 0.0005 | 42.9 | 33.4 |
| 0.0010 | 50.0 | 36.4 |
| 0.0020 | 54.6 | 38.1 |
| 0.0050 | 57.7 | 39.3 |
| 0.0100 | 58.9 | 39.7 |
| 0.0200 | 59.5 | 39.9 |
| 0.0500 | 59.8 | 40.0 |
| 0.1000 | 59.9 | 40.0 |
| 1.0000 | 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]).
A. competitive Incorrect B. contra-competitive Incorrect C. non-competitive Incorrect D. pre-competitive Incorrect E. un-competitive Correct MC6b1f
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 60.0 | 20.0 |
| 0.0002 | 90.0 | 30.0 |
| 0.0005 | 128.6 | 42.9 |
| 0.0010 | 150.0 | 50.0 |
| 0.0020 | 163.7 | 54.6 |
| 0.0050 | 173.1 | 57.7 |
| 0.0100 | 176.5 | 58.9 |
| 0.0200 | 178.3 | 59.5 |
| 0.0500 | 179.3 | 59.8 |
| 0.1000 | 179.7 | 59.9 |
| 1.0000 | 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]).
A. competitive Incorrect B. eco-competitive Incorrect C. non-competitive Correct D. quasi-competitive Incorrect E. un-competitive Incorrect MC6c65
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 33.4 | 18.2 |
| 0.0002 | 57.2 | 33.4 |
| 0.0005 | 100.0 | 66.7 |
| 0.0010 | 133.4 | 100.0 |
| 0.0020 | 160.0 | 133.4 |
| 0.0050 | 181.9 | 166.7 |
| 0.0100 | 190.5 | 181.9 |
| 0.0200 | 195.2 | 190.5 |
| 0.0500 | 198.1 | 196.1 |
| 0.1000 | 199.1 | 198.1 |
| 1.0000 | 200.0 | 199.9 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
A. competitive Correct B. extra-competitive Incorrect C. non-competitive Incorrect D. ultra-competitive Incorrect E. un-competitive Incorrect MC7154
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 1.2 | 0.4 |
| 0.0002 | 2.4 | 0.8 |
| 0.0005 | 5.5 | 1.9 |
| 0.0010 | 10.0 | 3.4 |
| 0.0020 | 17.2 | 5.8 |
| 0.0050 | 30.0 | 10.0 |
| 0.0100 | 40.0 | 13.4 |
| 0.0200 | 48.0 | 16.0 |
| 0.0500 | 54.6 | 18.2 |
| 0.1000 | 57.2 | 19.1 |
| 1.0000 | 59.8 | 20.0 |
| 10.0000 | 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]).
A. competitive Incorrect B. contra-competitive Incorrect C. non-competitive Correct D. super-competitive Incorrect E. un-competitive Incorrect MC7268
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 7.3 | 0.4 |
| 0.0002 | 13.4 | 0.8 |
| 0.0005 | 26.7 | 2.0 |
| 0.0010 | 40.0 | 3.9 |
| 0.0020 | 53.4 | 7.3 |
| 0.0050 | 66.7 | 16.0 |
| 0.0100 | 72.8 | 26.7 |
| 0.0200 | 76.2 | 40.0 |
| 0.0500 | 78.5 | 57.2 |
| 0.1000 | 79.3 | 66.7 |
| 1.0000 | 80.0 | 78.5 |
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]).
A. competitive Correct B. non-competitive Incorrect C. quasi-competitive Incorrect D. semi-competitive Incorrect E. un-competitive Incorrect MC72fa
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 0.8 | 0.4 |
| 0.0002 | 1.6 | 0.8 |
| 0.0005 | 3.7 | 1.9 |
| 0.0010 | 6.7 | 3.4 |
| 0.0020 | 11.5 | 5.8 |
| 0.0050 | 20.0 | 10.0 |
| 0.0100 | 26.7 | 13.4 |
| 0.0200 | 32.0 | 16.0 |
| 0.0500 | 36.4 | 18.2 |
| 0.1000 | 38.1 | 19.1 |
| 1.0000 | 39.9 | 20.0 |
| 10.0000 | 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]).
A. competitive Incorrect B. idio-competitive Incorrect C. non-competitive Correct D. supra-competitive Incorrect E. un-competitive Incorrect MC73ac
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 2.9 | 1.0 |
| 0.0002 | 5.5 | 1.9 |
| 0.0005 | 12.0 | 4.0 |
| 0.0010 | 20.0 | 6.7 |
| 0.0020 | 30.0 | 10.0 |
| 0.0050 | 42.9 | 14.3 |
| 0.0100 | 50.0 | 16.7 |
| 0.0200 | 54.6 | 18.2 |
| 0.0500 | 57.7 | 19.3 |
| 0.1000 | 58.9 | 19.7 |
| 1.0000 | 59.9 | 20.0 |
| 10.0000 | 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]).
A. competitive Incorrect B. non-competitive Correct C. post-competitive Incorrect D. self-competitive Incorrect E. un-competitive Incorrect MC7886
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 2.9 | 0.1 |
| 0.0002 | 5.5 | 0.2 |
| 0.0005 | 12.0 | 0.3 |
| 0.0010 | 20.0 | 0.6 |
| 0.0020 | 30.0 | 1.2 |
| 0.0050 | 42.9 | 2.9 |
| 0.0100 | 50.0 | 5.5 |
| 0.0200 | 54.6 | 10.0 |
| 0.0500 | 57.7 | 20.0 |
| 0.1000 | 58.9 | 30.0 |
| 1.0000 | 59.9 | 54.6 |
| 10.0000 | 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]).
A. competitive Correct B. mega-competitive Incorrect C. non-competitive Incorrect D. ortho-competitive Incorrect E. un-competitive Incorrect MC7d84
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 9.1 | 6.7 |
| 0.0002 | 16.7 | 11.5 |
| 0.0005 | 33.4 | 20.0 |
| 0.0010 | 50.0 | 26.7 |
| 0.0020 | 66.7 | 32.0 |
| 0.0050 | 83.4 | 36.4 |
| 0.0100 | 91.0 | 38.1 |
| 0.0200 | 95.3 | 39.1 |
| 0.0500 | 98.1 | 39.7 |
| 0.1000 | 99.1 | 39.9 |
| 1.0000 | 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]).
A. competitive Incorrect B. inter-competitive Incorrect C. non-competitive Incorrect D. supra-competitive Incorrect E. un-competitive Correct MC8570
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 5.8 | 5.5 |
| 0.0002 | 11.0 | 10.0 |
| 0.0005 | 24.0 | 20.0 |
| 0.0010 | 40.0 | 30.0 |
| 0.0020 | 60.0 | 40.0 |
| 0.0050 | 85.8 | 50.0 |
| 0.0100 | 100.0 | 54.6 |
| 0.0200 | 109.1 | 57.2 |
| 0.0500 | 115.4 | 58.9 |
| 0.1000 | 117.7 | 59.5 |
| 1.0000 | 119.8 | 60.0 |
| 10.0000 | 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]).
A. competitive Incorrect B. contra-competitive Incorrect C. inter-competitive Incorrect D. non-competitive Incorrect E. un-competitive Correct MC86de
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 13.4 | 6.7 |
| 0.0002 | 22.9 | 11.5 |
| 0.0005 | 40.0 | 20.0 |
| 0.0010 | 53.4 | 26.7 |
| 0.0020 | 64.0 | 32.0 |
| 0.0050 | 72.8 | 36.4 |
| 0.0100 | 76.2 | 38.1 |
| 0.0200 | 78.1 | 39.1 |
| 0.0500 | 79.3 | 39.7 |
| 0.1000 | 79.7 | 39.9 |
| 1.0000 | 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]).
A. competitive Incorrect B. dis-competitive Incorrect C. non-competitive Correct D. quasi-competitive Incorrect E. un-competitive Incorrect MC8931
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 4.0 | 0.2 |
| 0.0002 | 7.7 | 0.4 |
| 0.0005 | 18.2 | 1.0 |
| 0.0010 | 33.4 | 2.0 |
| 0.0020 | 57.2 | 4.0 |
| 0.0050 | 100.0 | 9.6 |
| 0.0100 | 133.4 | 18.2 |
| 0.0200 | 160.0 | 33.4 |
| 0.0500 | 181.9 | 66.7 |
| 0.1000 | 190.5 | 100.0 |
| 1.0000 | 199.1 | 181.9 |
| 10.0000 | 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]).
A. competitive Correct B. contra-competitive Incorrect C. non-competitive Incorrect D. post-competitive Incorrect E. un-competitive Incorrect MC8dbc
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 13.4 | 10.0 |
| 0.0002 | 20.0 | 13.4 |
| 0.0005 | 28.6 | 16.7 |
| 0.0010 | 33.4 | 18.2 |
| 0.0020 | 36.4 | 19.1 |
| 0.0050 | 38.5 | 19.7 |
| 0.0100 | 39.3 | 19.9 |
| 0.0200 | 39.7 | 20.0 |
| 0.0500 | 39.9 | 20.0 |
| 0.1000 | 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]).
A. competitive Incorrect B. iso-competitive Incorrect C. non-competitive Incorrect D. quasi-competitive Incorrect E. un-competitive Correct MC8e98
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 9.6 | 2.0 |
| 0.0002 | 18.2 | 4.0 |
| 0.0005 | 40.0 | 9.6 |
| 0.0010 | 66.7 | 18.2 |
| 0.0020 | 100.0 | 33.4 |
| 0.0050 | 142.9 | 66.7 |
| 0.0100 | 166.7 | 100.0 |
| 0.0200 | 181.9 | 133.4 |
| 0.0500 | 192.4 | 166.7 |
| 0.1000 | 196.1 | 181.9 |
| 1.0000 | 199.7 | 198.1 |
| 10.0000 | 200.0 | 199.9 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
A. competitive Correct B. non-competitive Incorrect C. oligo-competitive Incorrect D. supra-competitive Incorrect E. un-competitive Incorrect MC8e9a
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 30.0 | 26.7 |
| 0.0002 | 51.5 | 40.0 |
| 0.0005 | 90.0 | 57.2 |
| 0.0010 | 120.0 | 66.7 |
| 0.0020 | 144.0 | 72.8 |
| 0.0050 | 163.7 | 77.0 |
| 0.0100 | 171.5 | 78.5 |
| 0.0200 | 175.7 | 79.3 |
| 0.0500 | 178.3 | 79.7 |
| 0.1000 | 179.2 | 79.9 |
| 1.0000 | 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]).
A. competitive Incorrect B. dis-competitive Incorrect C. non-competitive Incorrect D. poly-competitive Incorrect E. un-competitive Correct MC8f35
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 14.6 | 13.4 |
| 0.0002 | 26.7 | 22.9 |
| 0.0005 | 53.4 | 40.0 |
| 0.0010 | 80.0 | 53.4 |
| 0.0020 | 106.7 | 64.0 |
| 0.0050 | 133.4 | 72.8 |
| 0.0100 | 145.5 | 76.2 |
| 0.0200 | 152.4 | 78.1 |
| 0.0500 | 156.9 | 79.3 |
| 0.1000 | 158.5 | 79.7 |
| 1.0000 | 159.9 | 80.0 |
| 10.0000 | 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]).
A. competitive Incorrect B. intra-competitive Incorrect C. mis-competitive Incorrect D. non-competitive Incorrect E. un-competitive Correct MC9010
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 4.8 | 2.0 |
| 0.0002 | 9.1 | 3.7 |
| 0.0005 | 20.0 | 8.0 |
| 0.0010 | 33.4 | 13.4 |
| 0.0020 | 50.0 | 20.0 |
| 0.0050 | 71.5 | 28.6 |
| 0.0100 | 83.4 | 33.4 |
| 0.0200 | 91.0 | 36.4 |
| 0.0500 | 96.2 | 38.5 |
| 0.1000 | 98.1 | 39.3 |
| 1.0000 | 99.9 | 40.0 |
| 10.0000 | 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]).
A. competitive Incorrect B. dis-competitive Incorrect C. non-competitive Correct D. self-competitive Incorrect E. un-competitive Incorrect MC9410
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 9.1 | 1.9 |
| 0.0002 | 16.7 | 3.4 |
| 0.0005 | 33.4 | 6.7 |
| 0.0010 | 50.0 | 10.0 |
| 0.0020 | 66.7 | 13.4 |
| 0.0050 | 83.4 | 16.7 |
| 0.0100 | 91.0 | 18.2 |
| 0.0200 | 95.3 | 19.1 |
| 0.0500 | 98.1 | 19.7 |
| 0.1000 | 99.1 | 19.9 |
| 1.0000 | 100.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
A. competitive Incorrect B. non-competitive Correct C. quasi-competitive Incorrect D. supra-competitive Incorrect E. un-competitive Incorrect MC941f
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 3.9 | 0.2 |
| 0.0002 | 7.3 | 0.4 |
| 0.0005 | 16.0 | 0.8 |
| 0.0010 | 26.7 | 1.6 |
| 0.0020 | 40.0 | 3.1 |
| 0.0050 | 57.2 | 7.3 |
| 0.0100 | 66.7 | 13.4 |
| 0.0200 | 72.8 | 22.9 |
| 0.0500 | 77.0 | 40.0 |
| 0.1000 | 78.5 | 53.4 |
| 1.0000 | 79.9 | 76.2 |
| 10.0000 | 80.0 | 79.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
A. anti-competitive Incorrect B. competitive Correct C. dis-competitive Incorrect D. non-competitive Incorrect E. un-competitive Incorrect MC9462
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 2.0 | 1.9 |
| 0.0002 | 3.7 | 3.4 |
| 0.0005 | 8.0 | 6.7 |
| 0.0010 | 13.4 | 10.0 |
| 0.0020 | 20.0 | 13.4 |
| 0.0050 | 28.6 | 16.7 |
| 0.0100 | 33.4 | 18.2 |
| 0.0200 | 36.4 | 19.1 |
| 0.0500 | 38.5 | 19.7 |
| 0.1000 | 39.3 | 19.9 |
| 1.0000 | 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]).
A. competitive Incorrect B. idio-competitive Incorrect C. non-competitive Incorrect D. ultra-competitive Incorrect E. un-competitive Correct MC9a24
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 3.6 | 2.0 |
| 0.0002 | 7.0 | 3.9 |
| 0.0005 | 16.4 | 9.1 |
| 0.0010 | 30.0 | 16.7 |
| 0.0020 | 51.5 | 28.6 |
| 0.0050 | 90.0 | 50.0 |
| 0.0100 | 120.1 | 66.7 |
| 0.0200 | 144.0 | 80.0 |
| 0.0500 | 163.7 | 91.0 |
| 0.1000 | 171.5 | 95.3 |
| 1.0000 | 179.2 | 99.6 |
| 10.0000 | 180.0 | 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]).
A. competitive Incorrect B. non-competitive Correct C. post-competitive Incorrect D. quasi-competitive Incorrect E. un-competitive Incorrect MC9d55
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 2.0 | 0.2 |
| 0.0002 | 3.9 | 0.4 |
| 0.0005 | 9.1 | 1.0 |
| 0.0010 | 16.7 | 2.0 |
| 0.0020 | 28.6 | 3.9 |
| 0.0050 | 50.0 | 9.1 |
| 0.0100 | 66.7 | 16.7 |
| 0.0200 | 80.0 | 28.6 |
| 0.0500 | 91.0 | 50.0 |
| 0.1000 | 95.3 | 66.7 |
| 1.0000 | 99.6 | 95.3 |
| 10.0000 | 100.0 | 99.6 |
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]).
A. competitive Correct B. epi-competitive Incorrect C. hetero-competitive Incorrect D. non-competitive Incorrect E. un-competitive Incorrect MC9e19
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 11.0 | 2.4 |
| 0.0002 | 20.0 | 4.7 |
| 0.0005 | 40.0 | 11.0 |
| 0.0010 | 60.0 | 20.0 |
| 0.0020 | 80.0 | 34.3 |
| 0.0050 | 100.0 | 60.0 |
| 0.0100 | 109.1 | 80.0 |
| 0.0200 | 114.3 | 96.0 |
| 0.0500 | 117.7 | 109.1 |
| 0.1000 | 118.9 | 114.3 |
| 1.0000 | 119.9 | 119.5 |
| 10.0000 | 120.0 | 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]).
A. competitive Correct B. non-competitive Incorrect C. ortho-competitive Incorrect D. pseudo-competitive Incorrect E. un-competitive Incorrect MC9efc
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 4.8 | 2.0 |
| 0.0002 | 9.1 | 3.9 |
| 0.0005 | 20.0 | 9.1 |
| 0.0010 | 33.4 | 16.7 |
| 0.0020 | 50.0 | 28.6 |
| 0.0050 | 71.5 | 50.0 |
| 0.0100 | 83.4 | 66.7 |
| 0.0200 | 91.0 | 80.0 |
| 0.0500 | 96.2 | 91.0 |
| 0.1000 | 98.1 | 95.3 |
| 1.0000 | 99.9 | 99.6 |
| 10.0000 | 100.0 | 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]).
A. competitive Correct B. inter-competitive Incorrect C. mega-competitive Incorrect D. non-competitive Incorrect E. un-competitive Incorrect MCa13e
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 2.0 | 0.8 |
| 0.0002 | 3.7 | 1.6 |
| 0.0005 | 8.0 | 3.7 |
| 0.0010 | 13.4 | 6.7 |
| 0.0020 | 20.0 | 11.5 |
| 0.0050 | 28.6 | 20.0 |
| 0.0100 | 33.4 | 26.7 |
| 0.0200 | 36.4 | 32.0 |
| 0.0500 | 38.5 | 36.4 |
| 0.1000 | 39.3 | 38.1 |
| 1.0000 | 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]).
A. competitive Correct B. non-competitive Incorrect C. over-competitive Incorrect D. ultra-competitive Incorrect E. un-competitive Incorrect MCa52a
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 18.2 | 4.0 |
| 0.0002 | 33.4 | 7.7 |
| 0.0005 | 66.7 | 18.2 |
| 0.0010 | 100.0 | 33.4 |
| 0.0020 | 133.4 | 57.2 |
| 0.0050 | 166.7 | 100.0 |
| 0.0100 | 181.9 | 133.4 |
| 0.0200 | 190.5 | 160.0 |
| 0.0500 | 196.1 | 181.9 |
| 0.1000 | 198.1 | 190.5 |
| 1.0000 | 199.9 | 199.1 |
| 10.0000 | 200.0 | 200.0 |
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]).
A. competitive Correct B. non-competitive Incorrect C. oligo-competitive Incorrect D. post-competitive Incorrect E. un-competitive Incorrect MCa571
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 13.4 | 13.4 |
| 0.0002 | 22.9 | 20.0 |
| 0.0005 | 40.0 | 28.6 |
| 0.0010 | 53.4 | 33.4 |
| 0.0020 | 64.0 | 36.4 |
| 0.0050 | 72.8 | 38.5 |
| 0.0100 | 76.2 | 39.3 |
| 0.0200 | 78.1 | 39.7 |
| 0.0500 | 79.3 | 39.9 |
| 0.1000 | 79.7 | 40.0 |
| 1.0000 | 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]).
A. competitive Incorrect B. hetero-competitive Incorrect C. hypo-competitive Incorrect D. non-competitive Incorrect E. un-competitive Correct MCa576
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 20.0 | 13.4 |
| 0.0002 | 34.3 | 20.0 |
| 0.0005 | 60.0 | 28.6 |
| 0.0010 | 80.0 | 33.4 |
| 0.0020 | 96.0 | 36.4 |
| 0.0050 | 109.1 | 38.5 |
| 0.0100 | 114.3 | 39.3 |
| 0.0200 | 117.1 | 39.7 |
| 0.0500 | 118.9 | 39.9 |
| 0.1000 | 119.5 | 40.0 |
| 1.0000 | 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]).
A. competitive Incorrect B. eco-competitive Incorrect C. mega-competitive Incorrect D. non-competitive Incorrect E. un-competitive Correct MCa5a3
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 10.0 | 6.7 |
| 0.0002 | 17.2 | 10.0 |
| 0.0005 | 30.0 | 14.3 |
| 0.0010 | 40.0 | 16.7 |
| 0.0020 | 48.0 | 18.2 |
| 0.0050 | 54.6 | 19.3 |
| 0.0100 | 57.2 | 19.7 |
| 0.0200 | 58.6 | 19.9 |
| 0.0500 | 59.5 | 20.0 |
| 0.1000 | 59.8 | 20.0 |
| 1.0000 | 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]).
A. competitive Incorrect B. epi-competitive Incorrect C. non-competitive Incorrect D. para-competitive Incorrect E. un-competitive Correct MCa63f
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 2.8 | 2.9 |
| 0.0002 | 5.4 | 5.5 |
| 0.0005 | 12.8 | 12.0 |
| 0.0010 | 23.4 | 20.0 |
| 0.0020 | 40.0 | 30.0 |
| 0.0050 | 70.0 | 42.9 |
| 0.0100 | 93.4 | 50.0 |
| 0.0200 | 112.0 | 54.6 |
| 0.0500 | 127.3 | 57.7 |
| 0.1000 | 133.4 | 58.9 |
| 1.0000 | 139.4 | 59.9 |
| 10.0000 | 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]).
A. competitive Incorrect B. epi-competitive Incorrect C. inter-competitive Incorrect D. non-competitive Incorrect E. un-competitive Correct MCa70c
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 60.0 | 0.4 |
| 0.0002 | 90.0 | 0.8 |
| 0.0005 | 128.6 | 1.8 |
| 0.0010 | 150.0 | 3.6 |
| 0.0020 | 163.7 | 7.0 |
| 0.0050 | 173.1 | 16.4 |
| 0.0100 | 176.5 | 30.0 |
| 0.0200 | 178.3 | 51.5 |
| 0.0500 | 179.3 | 90.0 |
| 0.1000 | 179.7 | 120.0 |
| 1.0000 | 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]).
A. auto-competitive Incorrect B. competitive Correct C. hyper-competitive Incorrect D. non-competitive Incorrect E. un-competitive Incorrect MCa967
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 9.6 | 5.8 |
| 0.0002 | 18.2 | 11.0 |
| 0.0005 | 40.0 | 24.0 |
| 0.0010 | 66.7 | 40.0 |
| 0.0020 | 100.0 | 60.0 |
| 0.0050 | 142.9 | 85.8 |
| 0.0100 | 166.7 | 100.0 |
| 0.0200 | 181.9 | 109.1 |
| 0.0500 | 192.4 | 115.4 |
| 0.1000 | 196.1 | 117.7 |
| 1.0000 | 199.7 | 119.8 |
| 10.0000 | 200.0 | 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]).
A. competitive Incorrect B. eco-competitive Incorrect C. non-competitive Correct D. oligo-competitive Incorrect E. un-competitive Incorrect MCab0a
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 5.5 | 3.7 |
| 0.0002 | 10.0 | 6.7 |
| 0.0005 | 20.0 | 13.4 |
| 0.0010 | 30.0 | 20.0 |
| 0.0020 | 40.0 | 26.7 |
| 0.0050 | 50.0 | 33.4 |
| 0.0100 | 54.6 | 36.4 |
| 0.0200 | 57.2 | 38.1 |
| 0.0500 | 58.9 | 39.3 |
| 0.1000 | 59.5 | 39.7 |
| 1.0000 | 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]).
A. anti-competitive Incorrect B. competitive Incorrect C. hyper-competitive Incorrect D. non-competitive Correct E. un-competitive Incorrect MCad4d
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 26.7 | 0.8 |
| 0.0002 | 40.0 | 1.6 |
| 0.0005 | 57.2 | 3.9 |
| 0.0010 | 66.7 | 7.3 |
| 0.0020 | 72.8 | 13.4 |
| 0.0050 | 77.0 | 26.7 |
| 0.0100 | 78.5 | 40.0 |
| 0.0200 | 79.3 | 53.4 |
| 0.0500 | 79.7 | 66.7 |
| 0.1000 | 79.9 | 72.8 |
| 1.0000 | 80.0 | 79.3 |
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]).
A. competitive Correct B. iso-competitive Incorrect C. mis-competitive Incorrect D. non-competitive Incorrect E. un-competitive Incorrect MCb66e
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 20.0 | 0.1 |
| 0.0002 | 30.0 | 0.2 |
| 0.0005 | 42.9 | 0.3 |
| 0.0010 | 50.0 | 0.6 |
| 0.0020 | 54.6 | 1.2 |
| 0.0050 | 57.7 | 2.9 |
| 0.0100 | 58.9 | 5.5 |
| 0.0200 | 59.5 | 10.0 |
| 0.0500 | 59.8 | 20.0 |
| 0.1000 | 59.9 | 30.0 |
| 1.0000 | 60.0 | 54.6 |
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]).
A. competitive Correct B. hypo-competitive Incorrect C. non-competitive Incorrect D. pre-competitive Incorrect E. un-competitive Incorrect MCbad1
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 8.6 | 7.7 |
| 0.0002 | 16.4 | 14.6 |
| 0.0005 | 36.0 | 32.0 |
| 0.0010 | 60.0 | 53.4 |
| 0.0020 | 90.0 | 80.0 |
| 0.0050 | 128.6 | 114.3 |
| 0.0100 | 150.0 | 133.4 |
| 0.0200 | 163.7 | 145.5 |
| 0.0500 | 173.1 | 153.9 |
| 0.1000 | 176.5 | 156.9 |
| 1.0000 | 179.7 | 159.7 |
| 10.0000 | 180.0 | 160.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
A. competitive Incorrect B. iso-competitive Incorrect C. non-competitive Correct D. oligo-competitive Incorrect E. un-competitive Incorrect MCbb4e
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 8.6 | 3.6 |
| 0.0002 | 16.4 | 7.0 |
| 0.0005 | 36.0 | 16.4 |
| 0.0010 | 60.0 | 30.0 |
| 0.0020 | 90.0 | 51.5 |
| 0.0050 | 128.6 | 90.0 |
| 0.0100 | 150.0 | 120.1 |
| 0.0200 | 163.7 | 144.0 |
| 0.0500 | 173.1 | 163.7 |
| 0.1000 | 176.5 | 171.5 |
| 1.0000 | 179.7 | 179.2 |
| 10.0000 | 180.0 | 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]).
A. competitive Correct B. non-competitive Incorrect C. proto-competitive Incorrect D. quasi-competitive Incorrect E. un-competitive Incorrect MCbb5d
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 13.4 | 3.7 |
| 0.0002 | 20.0 | 6.7 |
| 0.0005 | 28.6 | 13.4 |
| 0.0010 | 33.4 | 20.0 |
| 0.0020 | 36.4 | 26.7 |
| 0.0050 | 38.5 | 33.4 |
| 0.0100 | 39.3 | 36.4 |
| 0.0200 | 39.7 | 38.1 |
| 0.0500 | 39.9 | 39.3 |
| 0.1000 | 40.0 | 39.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
A. anti-competitive Incorrect B. auto-competitive Incorrect C. competitive Correct D. non-competitive Incorrect E. un-competitive Incorrect MCbf87
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 53.4 | 0.2 |
| 0.0002 | 80.0 | 0.4 |
| 0.0005 | 114.3 | 0.8 |
| 0.0010 | 133.4 | 1.6 |
| 0.0020 | 145.5 | 3.2 |
| 0.0050 | 153.9 | 7.7 |
| 0.0100 | 156.9 | 14.6 |
| 0.0200 | 158.5 | 26.7 |
| 0.0500 | 159.4 | 53.4 |
| 0.1000 | 159.7 | 80.0 |
| 1.0000 | 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]).
A. competitive Correct B. hyper-competitive Incorrect C. non-competitive Incorrect D. para-competitive Incorrect E. un-competitive Incorrect MCbfba
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 33.4 | 26.7 |
| 0.0002 | 57.2 | 40.0 |
| 0.0005 | 100.0 | 57.2 |
| 0.0010 | 133.4 | 66.7 |
| 0.0020 | 160.0 | 72.8 |
| 0.0050 | 181.9 | 77.0 |
| 0.0100 | 190.5 | 78.5 |
| 0.0200 | 195.2 | 79.3 |
| 0.0500 | 198.1 | 79.7 |
| 0.1000 | 199.1 | 79.9 |
| 1.0000 | 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]).
A. auto-competitive Incorrect B. competitive Incorrect C. non-competitive Incorrect D. super-competitive Incorrect E. un-competitive Correct MCc023
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 46.7 | 26.7 |
| 0.0002 | 70.0 | 40.0 |
| 0.0005 | 100.1 | 57.2 |
| 0.0010 | 116.7 | 66.7 |
| 0.0020 | 127.3 | 72.8 |
| 0.0050 | 134.7 | 77.0 |
| 0.0100 | 137.3 | 78.5 |
| 0.0200 | 138.7 | 79.3 |
| 0.0500 | 139.5 | 79.7 |
| 0.1000 | 139.8 | 79.9 |
| 1.0000 | 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]).
A. competitive Incorrect B. hypo-competitive Incorrect C. non-competitive Correct D. supra-competitive Incorrect E. un-competitive Incorrect MCc243
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 1.6 | 0.4 |
| 0.0002 | 3.1 | 0.8 |
| 0.0005 | 7.3 | 2.0 |
| 0.0010 | 13.4 | 3.9 |
| 0.0020 | 22.9 | 7.3 |
| 0.0050 | 40.0 | 16.0 |
| 0.0100 | 53.4 | 26.7 |
| 0.0200 | 64.0 | 40.0 |
| 0.0500 | 72.8 | 57.2 |
| 0.1000 | 76.2 | 66.7 |
| 1.0000 | 79.7 | 78.5 |
| 10.0000 | 80.0 | 79.9 |
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]).
A. competitive Correct B. homo-competitive Incorrect C. non-competitive Incorrect D. pre-competitive Incorrect E. un-competitive Incorrect MCc413
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 14.6 | 3.2 |
| 0.0002 | 26.7 | 6.2 |
| 0.0005 | 53.4 | 14.6 |
| 0.0010 | 80.0 | 26.7 |
| 0.0020 | 106.7 | 45.8 |
| 0.0050 | 133.4 | 80.0 |
| 0.0100 | 145.5 | 106.7 |
| 0.0200 | 152.4 | 128.0 |
| 0.0500 | 156.9 | 145.5 |
| 0.1000 | 158.5 | 152.4 |
| 1.0000 | 159.9 | 159.3 |
| 10.0000 | 160.0 | 160.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
A. competitive Correct B. hetero-competitive Incorrect C. hypo-competitive Incorrect D. non-competitive Incorrect E. un-competitive Incorrect MCc5d0
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 5.5 | 6.7 |
| 0.0002 | 10.0 | 11.5 |
| 0.0005 | 20.0 | 20.0 |
| 0.0010 | 30.0 | 26.7 |
| 0.0020 | 40.0 | 32.0 |
| 0.0050 | 50.0 | 36.4 |
| 0.0100 | 54.6 | 38.1 |
| 0.0200 | 57.2 | 39.1 |
| 0.0500 | 58.9 | 39.7 |
| 0.1000 | 59.5 | 39.9 |
| 1.0000 | 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]).
A. auto-competitive Incorrect B. competitive Incorrect C. iso-competitive Incorrect D. non-competitive Incorrect E. un-competitive Correct MCc832
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 26.7 | 3.4 |
| 0.0002 | 45.8 | 5.8 |
| 0.0005 | 80.0 | 10.0 |
| 0.0010 | 106.7 | 13.4 |
| 0.0020 | 128.0 | 16.0 |
| 0.0050 | 145.5 | 18.2 |
| 0.0100 | 152.4 | 19.1 |
| 0.0200 | 156.1 | 19.6 |
| 0.0500 | 158.5 | 19.9 |
| 0.1000 | 159.3 | 20.0 |
| 1.0000 | 160.0 | 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]).
A. competitive Incorrect B. non-competitive Correct C. ortho-competitive Incorrect D. proto-competitive Incorrect E. un-competitive Incorrect MCcd9c
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 20.0 | 6.7 |
| 0.0002 | 30.0 | 10.0 |
| 0.0005 | 42.9 | 14.3 |
| 0.0010 | 50.0 | 16.7 |
| 0.0020 | 54.6 | 18.2 |
| 0.0050 | 57.7 | 19.3 |
| 0.0100 | 58.9 | 19.7 |
| 0.0200 | 59.5 | 19.9 |
| 0.0500 | 59.8 | 20.0 |
| 0.1000 | 59.9 | 20.0 |
| 1.0000 | 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]).
A. competitive Incorrect B. intra-competitive Incorrect C. non-competitive Correct D. self-competitive Incorrect E. un-competitive Incorrect MCd171
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 6.7 | 2.8 |
| 0.0002 | 12.8 | 5.4 |
| 0.0005 | 28.1 | 12.8 |
| 0.0010 | 46.7 | 23.4 |
| 0.0020 | 70.0 | 40.0 |
| 0.0050 | 100.1 | 70.0 |
| 0.0100 | 116.7 | 93.4 |
| 0.0200 | 127.3 | 112.0 |
| 0.0500 | 134.7 | 127.3 |
| 0.1000 | 137.3 | 133.4 |
| 1.0000 | 139.8 | 139.4 |
| 10.0000 | 140.0 | 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]).
A. anti-competitive Incorrect B. competitive Correct C. non-competitive Incorrect D. over-competitive Incorrect E. un-competitive Incorrect MCd3fd
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 11.0 | 9.1 |
| 0.0002 | 20.0 | 16.7 |
| 0.0005 | 40.0 | 33.4 |
| 0.0010 | 60.0 | 50.0 |
| 0.0020 | 80.0 | 66.7 |
| 0.0050 | 100.0 | 83.4 |
| 0.0100 | 109.1 | 91.0 |
| 0.0200 | 114.3 | 95.3 |
| 0.0500 | 117.7 | 98.1 |
| 0.1000 | 118.9 | 99.1 |
| 1.0000 | 119.9 | 100.0 |
| 10.0000 | 120.0 | 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]).
A. competitive Incorrect B. non-competitive Correct C. oligo-competitive Incorrect D. para-competitive Incorrect E. un-competitive Incorrect MCd5c9
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 26.7 | 20.0 |
| 0.0002 | 45.8 | 30.0 |
| 0.0005 | 80.0 | 42.9 |
| 0.0010 | 106.7 | 50.0 |
| 0.0020 | 128.0 | 54.6 |
| 0.0050 | 145.5 | 57.7 |
| 0.0100 | 152.4 | 58.9 |
| 0.0200 | 156.1 | 59.5 |
| 0.0500 | 158.5 | 59.8 |
| 0.1000 | 159.3 | 59.9 |
| 1.0000 | 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]).
A. competitive Incorrect B. hyper-competitive Incorrect C. non-competitive Incorrect D. over-competitive Incorrect E. un-competitive Correct MCd730
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 16.4 | 5.5 |
| 0.0002 | 30.0 | 10.0 |
| 0.0005 | 60.0 | 20.0 |
| 0.0010 | 90.0 | 30.0 |
| 0.0020 | 120.0 | 40.0 |
| 0.0050 | 150.0 | 50.0 |
| 0.0100 | 163.7 | 54.6 |
| 0.0200 | 171.5 | 57.2 |
| 0.0500 | 176.5 | 58.9 |
| 0.1000 | 178.3 | 59.5 |
| 1.0000 | 179.9 | 60.0 |
| 10.0000 | 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]).
A. competitive Incorrect B. eco-competitive Incorrect C. non-competitive Correct D. ortho-competitive Incorrect E. un-competitive Incorrect MCd85c
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 3.9 | 2.0 |
| 0.0002 | 7.3 | 3.7 |
| 0.0005 | 16.0 | 8.0 |
| 0.0010 | 26.7 | 13.4 |
| 0.0020 | 40.0 | 20.0 |
| 0.0050 | 57.2 | 28.6 |
| 0.0100 | 66.7 | 33.4 |
| 0.0200 | 72.8 | 36.4 |
| 0.0500 | 77.0 | 38.5 |
| 0.1000 | 78.5 | 39.3 |
| 1.0000 | 79.9 | 40.0 |
| 10.0000 | 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]).
A. auto-competitive Incorrect B. competitive Incorrect C. non-competitive Correct D. over-competitive Incorrect E. un-competitive Incorrect MCd951
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 5.5 | 0.3 |
| 0.0002 | 10.0 | 0.6 |
| 0.0005 | 20.0 | 1.5 |
| 0.0010 | 30.0 | 2.9 |
| 0.0020 | 40.0 | 5.5 |
| 0.0050 | 50.0 | 12.0 |
| 0.0100 | 54.6 | 20.0 |
| 0.0200 | 57.2 | 30.0 |
| 0.0500 | 58.9 | 42.9 |
| 0.1000 | 59.5 | 50.0 |
| 1.0000 | 60.0 | 58.9 |
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]).
A. competitive Correct B. hyper-competitive Incorrect C. non-competitive Incorrect D. ultra-competitive Incorrect E. un-competitive Incorrect MCdf7b
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 3.2 | 2.9 |
| 0.0002 | 6.2 | 5.5 |
| 0.0005 | 14.6 | 12.0 |
| 0.0010 | 26.7 | 20.0 |
| 0.0020 | 45.8 | 30.0 |
| 0.0050 | 80.0 | 42.9 |
| 0.0100 | 106.7 | 50.0 |
| 0.0200 | 128.0 | 54.6 |
| 0.0500 | 145.5 | 57.7 |
| 0.1000 | 152.4 | 58.9 |
| 1.0000 | 159.3 | 59.9 |
| 10.0000 | 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]).
A. competitive Incorrect B. idio-competitive Incorrect C. non-competitive Incorrect D. pseudo-competitive Incorrect E. un-competitive Correct MCdf98
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 4.0 | 3.9 |
| 0.0002 | 7.7 | 7.3 |
| 0.0005 | 18.2 | 16.0 |
| 0.0010 | 33.4 | 26.7 |
| 0.0020 | 57.2 | 40.0 |
| 0.0050 | 100.0 | 57.2 |
| 0.0100 | 133.4 | 66.7 |
| 0.0200 | 160.0 | 72.8 |
| 0.0500 | 181.9 | 77.0 |
| 0.1000 | 190.5 | 78.5 |
| 1.0000 | 199.1 | 79.9 |
| 10.0000 | 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]).
A. competitive Incorrect B. dis-competitive Incorrect C. eco-competitive Incorrect D. non-competitive Incorrect E. un-competitive Correct MCe167
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 1.2 | 0.6 |
| 0.0002 | 2.4 | 1.2 |
| 0.0005 | 5.5 | 2.9 |
| 0.0010 | 10.0 | 5.5 |
| 0.0020 | 17.2 | 10.0 |
| 0.0050 | 30.0 | 20.0 |
| 0.0100 | 40.0 | 30.0 |
| 0.0200 | 48.0 | 40.0 |
| 0.0500 | 54.6 | 50.0 |
| 0.1000 | 57.2 | 54.6 |
| 1.0000 | 59.8 | 59.5 |
| 10.0000 | 60.0 | 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]).
A. competitive Correct B. epi-competitive Incorrect C. non-competitive Incorrect D. ortho-competitive Incorrect E. un-competitive Incorrect MCe28c
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 5.8 | 3.9 |
| 0.0002 | 11.0 | 7.3 |
| 0.0005 | 24.0 | 16.0 |
| 0.0010 | 40.0 | 26.7 |
| 0.0020 | 60.0 | 40.0 |
| 0.0050 | 85.8 | 57.2 |
| 0.0100 | 100.0 | 66.7 |
| 0.0200 | 109.1 | 72.8 |
| 0.0500 | 115.4 | 77.0 |
| 0.1000 | 117.7 | 78.5 |
| 1.0000 | 119.8 | 79.9 |
| 10.0000 | 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]).
A. competitive Incorrect B. iso-competitive Incorrect C. non-competitive Correct D. oligo-competitive Incorrect E. un-competitive Incorrect MCe3f5
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 7.3 | 6.7 |
| 0.0002 | 13.4 | 11.5 |
| 0.0005 | 26.7 | 20.0 |
| 0.0010 | 40.0 | 26.7 |
| 0.0020 | 53.4 | 32.0 |
| 0.0050 | 66.7 | 36.4 |
| 0.0100 | 72.8 | 38.1 |
| 0.0200 | 76.2 | 39.1 |
| 0.0500 | 78.5 | 39.7 |
| 0.1000 | 79.3 | 39.9 |
| 1.0000 | 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]).
A. competitive Incorrect B. hypo-competitive Incorrect C. intra-competitive Incorrect D. non-competitive Incorrect E. un-competitive Correct MCe48d
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 66.7 | 50.0 |
| 0.0002 | 100.0 | 66.7 |
| 0.0005 | 142.9 | 83.4 |
| 0.0010 | 166.7 | 91.0 |
| 0.0020 | 181.9 | 95.3 |
| 0.0050 | 192.4 | 98.1 |
| 0.0100 | 196.1 | 99.1 |
| 0.0200 | 198.1 | 99.6 |
| 0.0500 | 199.3 | 99.9 |
| 0.1000 | 199.7 | 100.0 |
| 1.0000 | 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]).
A. competitive Incorrect B. inter-competitive Incorrect C. mis-competitive Incorrect D. non-competitive Incorrect E. un-competitive Correct MCe4f5
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 4.0 | 2.0 |
| 0.0002 | 7.7 | 3.9 |
| 0.0005 | 18.2 | 9.1 |
| 0.0010 | 33.4 | 16.7 |
| 0.0020 | 57.2 | 28.6 |
| 0.0050 | 100.0 | 50.0 |
| 0.0100 | 133.4 | 66.7 |
| 0.0200 | 160.0 | 80.0 |
| 0.0500 | 181.9 | 91.0 |
| 0.1000 | 190.5 | 95.3 |
| 1.0000 | 199.1 | 99.6 |
| 10.0000 | 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]).
A. competitive Incorrect B. non-competitive Correct C. self-competitive Incorrect D. supra-competitive Incorrect E. un-competitive Incorrect MCeccd
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 0.8 | 0.1 |
| 0.0002 | 1.6 | 0.1 |
| 0.0005 | 3.7 | 0.2 |
| 0.0010 | 6.7 | 0.4 |
| 0.0020 | 11.5 | 0.8 |
| 0.0050 | 20.0 | 2.0 |
| 0.0100 | 26.7 | 3.7 |
| 0.0200 | 32.0 | 6.7 |
| 0.0500 | 36.4 | 13.4 |
| 0.1000 | 38.1 | 20.0 |
| 1.0000 | 39.9 | 36.4 |
| 10.0000 | 40.0 | 39.7 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
A. competitive Correct B. mega-competitive Incorrect C. non-competitive Incorrect D. over-competitive Incorrect E. un-competitive Incorrect MCefdb
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 3.7 | 0.1 |
| 0.0002 | 6.7 | 0.2 |
| 0.0005 | 13.4 | 0.4 |
| 0.0010 | 20.0 | 0.8 |
| 0.0020 | 26.7 | 1.6 |
| 0.0050 | 33.4 | 3.7 |
| 0.0100 | 36.4 | 6.7 |
| 0.0200 | 38.1 | 11.5 |
| 0.0500 | 39.3 | 20.0 |
| 0.1000 | 39.7 | 26.7 |
| 1.0000 | 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]).
A. competitive Correct B. extra-competitive Incorrect C. non-competitive Incorrect D. para-competitive Incorrect E. un-competitive Incorrect MCf065
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 33.4 | 6.7 |
| 0.0002 | 50.0 | 10.0 |
| 0.0005 | 71.5 | 14.3 |
| 0.0010 | 83.4 | 16.7 |
| 0.0020 | 91.0 | 18.2 |
| 0.0050 | 96.2 | 19.3 |
| 0.0100 | 98.1 | 19.7 |
| 0.0200 | 99.1 | 19.9 |
| 0.0500 | 99.7 | 20.0 |
| 0.1000 | 99.9 | 20.0 |
| 1.0000 | 100.0 | 20.0 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
A. competitive Incorrect B. idio-competitive Incorrect C. non-competitive Correct D. para-competitive Incorrect E. un-competitive Incorrect MCf4a8
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 2.4 | 2.0 |
| 0.0002 | 4.7 | 3.7 |
| 0.0005 | 11.0 | 8.0 |
| 0.0010 | 20.0 | 13.4 |
| 0.0020 | 34.3 | 20.0 |
| 0.0050 | 60.0 | 28.6 |
| 0.0100 | 80.0 | 33.4 |
| 0.0200 | 96.0 | 36.4 |
| 0.0500 | 109.1 | 38.5 |
| 0.1000 | 114.3 | 39.3 |
| 1.0000 | 119.5 | 40.0 |
| 10.0000 | 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]).
A. auto-competitive Incorrect B. competitive Incorrect C. homo-competitive Incorrect D. non-competitive Incorrect E. un-competitive Correct MCf736
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 10.0 | 1.2 |
| 0.0002 | 17.2 | 2.4 |
| 0.0005 | 30.0 | 5.5 |
| 0.0010 | 40.0 | 10.0 |
| 0.0020 | 48.0 | 17.2 |
| 0.0050 | 54.6 | 30.0 |
| 0.0100 | 57.2 | 40.0 |
| 0.0200 | 58.6 | 48.0 |
| 0.0500 | 59.5 | 54.6 |
| 0.1000 | 59.8 | 57.2 |
| 1.0000 | 60.0 | 59.8 |
Based on the data provided, determine the type of inhibition show by the inhibitor. Consider how the addition of the inhibitor affects the initial reaction velocities (V0) at various substrate concentrations ([S]).
A. competitive Correct B. non-competitive Incorrect C. over-competitive Incorrect D. proto-competitive Incorrect E. un-competitive Incorrect MCf976
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 2.4 | 0.4 |
| 0.0002 | 4.7 | 0.8 |
| 0.0005 | 11.0 | 1.9 |
| 0.0010 | 20.0 | 3.4 |
| 0.0020 | 34.3 | 5.8 |
| 0.0050 | 60.0 | 10.0 |
| 0.0100 | 80.0 | 13.4 |
| 0.0200 | 96.0 | 16.0 |
| 0.0500 | 109.1 | 18.2 |
| 0.1000 | 114.3 | 19.1 |
| 1.0000 | 119.5 | 20.0 |
| 10.0000 | 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]).
A. competitive Incorrect B. inter-competitive Incorrect C. mega-competitive Incorrect D. non-competitive Correct E. un-competitive Incorrect MCfefa
Michaelis-Menten Kinetics and Inhibition Type Determination
The table below presents data on enzyme activity measured as initial reaction velocities (V0) with and without the presence of an inhibitor at various substrate concentrations ([S]).
| substrate concentration, [S] | initial reaction velocity no inhibitor V0 (–inh) | initial reaction velocity with inhibitor V0 (+inh) |
|---|---|---|
| 0.0001 | 1.6 | 0.8 |
| 0.0002 | 3.1 | 1.6 |
| 0.0005 | 7.3 | 3.7 |
| 0.0010 | 13.4 | 6.7 |
| 0.0020 | 22.9 | 11.5 |
| 0.0050 | 40.0 | 20.0 |
| 0.0100 | 53.4 | 26.7 |
| 0.0200 | 64.0 | 32.0 |
| 0.0500 | 72.8 | 36.4 |
| 0.1000 | 76.2 | 38.1 |
| 1.0000 | 79.7 | 39.9 |
| 10.0000 | 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]).
A. competitive Incorrect B. mega-competitive Incorrect C. non-competitive Correct D. ortho-competitive Incorrect E. un-competitive Incorrect