1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in each reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 UM. a Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3). d. Calculate the reaction Kcat for the Control in experiment (1). Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and K for the enzyme. c. e. [S] (mM) (1) V. [(umol/(ml.s)) (2) v. (umol/(ml.s)] (3) V. {lumol/(ml.s)] 7.6 4.4 6.6 4 14.6 8.6 11.4 26.6 16.4 29.8 40.8 17.8 16 45.8 24.6 24 60 28.2 |লন
1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in each reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 UM. a Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3). d. Calculate the reaction Kcat for the Control in experiment (1). Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and K for the enzyme. c. e. [S] (mM) (1) V. [(umol/(ml.s)) (2) v. (umol/(ml.s)] (3) V. {lumol/(ml.s)] 7.6 4.4 6.6 4 14.6 8.6 11.4 26.6 16.4 29.8 40.8 17.8 16 45.8 24.6 24 60 28.2 |লন
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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![1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two
columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in each
reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001
UM.
a Calculate both Vmax and KM for the control using Lineweaver-Burk curve.
b. Provide the type of inhibition for both?
Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3).
d. Calculate the reaction Kcat for the Control in experiment (1).
Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax
and K for the enzyme.
c.
e.
[S] (mM)
(1) V.
[(umol/(ml.s))
(2) v.
(umol/(ml.s)]
(3) V.
{lumol/(ml.s)]
7.6
4.4
6.6
4
14.6
8.6
11.4
26.6
16.4
29.8
40.8
17.8
16
45.8
24.6
24
60
28.2
|লন](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F890b21c0-0748-4ed4-829a-7a2c6d922d1c%2Fc38e0dde-5145-4ed7-b5f5-d56b76c16e9d%2Fdtt49nw.jpeg&w=3840&q=75)
Transcribed Image Text:1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two
columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in each
reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001
UM.
a Calculate both Vmax and KM for the control using Lineweaver-Burk curve.
b. Provide the type of inhibition for both?
Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3).
d. Calculate the reaction Kcat for the Control in experiment (1).
Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax
and K for the enzyme.
c.
e.
[S] (mM)
(1) V.
[(umol/(ml.s))
(2) v.
(umol/(ml.s)]
(3) V.
{lumol/(ml.s)]
7.6
4.4
6.6
4
14.6
8.6
11.4
26.6
16.4
29.8
40.8
17.8
16
45.8
24.6
24
60
28.2
|লন
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