A kinetic study of an intestinal peptidase using glycylglycine as the substrate produced the experimental data shown in the table. glycylglycine + H,O 2 glycine [S] (mM) Product formed (umol min) 1.5 0.21 2.0 0.24 3.0 0.28 4.0 0.33 8.0 0.40 16.0 0.45 Calculate the standard error of regression (SER) for the Lineweaver-Burk slope and the Eadie-Hofstee slope to compare the precision of cach. Lineweaver-Burk SER: Jumol min- jumol min Eadie-Hofstee SER:

Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
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14
A kinetic study of an intestinal peptidase using glycylglycine as the substrate produced the experimental data shown in the table.
glycylglycine + H,O -
2 glycine
[S] (mM)
Product formed (umol min)
1.5
0.21
2.0
0.24
3.0
0.28
4.0
0.33
8.0
0.40
16.0
0.45
Calculate the standard error of regression (SER) for the Lineweaver-Burk slope and the Eadie-Hofstee slope to compare the
precision of cach.
umol min"
Lineweaver-Burk SER:
umol min-
Eadie-Hofstee SER:
Transcribed Image Text:A kinetic study of an intestinal peptidase using glycylglycine as the substrate produced the experimental data shown in the table. glycylglycine + H,O - 2 glycine [S] (mM) Product formed (umol min) 1.5 0.21 2.0 0.24 3.0 0.28 4.0 0.33 8.0 0.40 16.0 0.45 Calculate the standard error of regression (SER) for the Lineweaver-Burk slope and the Eadie-Hofstee slope to compare the precision of cach. umol min" Lineweaver-Burk SER: umol min- Eadie-Hofstee SER:
84.5%
Resources
O Hint
Check Answe
There are several ways to transform the Michaelis-Menten
equation so as to plot data and derive kinetic parameters, cach
with different advantages depending on the data set being
analyzed. One transformation of the Michaelis-Menten
equation is the Lineweaver-Burk, or double-reciprocal,
equation. Multiplying both sides of the Lineweaver-Burk
equation by Vmax and rearranging gives the
Eadie-Hofstee equation.
Slope = -K
Vo
+ Vmax
[S]
Vo = - (K)
Vo
for an enzyme-catalyzed
[S]
Consider the plot of Va versus
reaction. The control reactions (blue curve) did not contain
any inhibitor.
[S]
Which of the other curves (A, B, or C) depicts this enzyme's activity in the presence of a competitive inhibitor?
curve A
curve C
curve B
Transcribed Image Text:84.5% Resources O Hint Check Answe There are several ways to transform the Michaelis-Menten equation so as to plot data and derive kinetic parameters, cach with different advantages depending on the data set being analyzed. One transformation of the Michaelis-Menten equation is the Lineweaver-Burk, or double-reciprocal, equation. Multiplying both sides of the Lineweaver-Burk equation by Vmax and rearranging gives the Eadie-Hofstee equation. Slope = -K Vo + Vmax [S] Vo = - (K) Vo for an enzyme-catalyzed [S] Consider the plot of Va versus reaction. The control reactions (blue curve) did not contain any inhibitor. [S] Which of the other curves (A, B, or C) depicts this enzyme's activity in the presence of a competitive inhibitor? curve A curve C curve B
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