Kinetic measurements using a constant concentration of enzyme and various concentrations of S are summarized below. Draw plots of these data according to (a) Michaelis-Menton, (b) Lineweaver-Burke and (c) Eadie-Hofstee equations. Compare the resulting K and Vmax values for each. Substrate (M) 4.00 X 10 2.00 X 104 1.00 X 10 0.50 X 104 0.40 X 104 v. (jmol/min) 140 115 81 62 55

Chemistry & Chemical Reactivity
10th Edition
ISBN:9781337399074
Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel
Publisher:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel
Chapter14: Chemical Kinetics: The Rates Of Chemical Reactions
Section14.7: Reaction Mechanisms
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Kinetic measurements using a constant concentration of enzyme and various concentrations of S are
summarized below. Draw plots of these data according to (a) Michaelis-Menton, (b) Lineweaver-Burke
and (c) Eadie-Hofstee equations. Compare the resulting K. and Vmx values for each.
Substrate (M)
4.00 X 104
2.00 X 104
v (mol/min)
140
115
1.00 X 104
81
0.50 X 104
0.40 X 104
0.25 X 104
0.20 X 104
62
55
36
31
Transcribed Image Text:Kinetic measurements using a constant concentration of enzyme and various concentrations of S are summarized below. Draw plots of these data according to (a) Michaelis-Menton, (b) Lineweaver-Burke and (c) Eadie-Hofstee equations. Compare the resulting K. and Vmx values for each. Substrate (M) 4.00 X 104 2.00 X 104 v (mol/min) 140 115 1.00 X 104 81 0.50 X 104 0.40 X 104 0.25 X 104 0.20 X 104 62 55 36 31
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