A kinetic study of an intestinal peptidase using glycylglycine as the substrate produced the experimental data shown in the table. glycylglycine + H₂O → 2 glycine [S] (mm) 1.5 2.0 3.0 4.0 8.0 16.0 Calculate the standard error of regression (SER) for the Lineweaver-Burk slope and the Eadie-Hofstee slope to compare the precision of each. Lineweaver-Burk SER: Eadie Hofstee SER: Product formed (µmol min-¹) 0.21 0.24 0.28 0.33 0.40 0.45 Incorrect 0.182 0.128 μmol min μmol min -1
A kinetic study of an intestinal peptidase using glycylglycine as the substrate produced the experimental data shown in the table. glycylglycine + H₂O → 2 glycine [S] (mm) 1.5 2.0 3.0 4.0 8.0 16.0 Calculate the standard error of regression (SER) for the Lineweaver-Burk slope and the Eadie-Hofstee slope to compare the precision of each. Lineweaver-Burk SER: Eadie Hofstee SER: Product formed (µmol min-¹) 0.21 0.24 0.28 0.33 0.40 0.45 Incorrect 0.182 0.128 μmol min μmol min -1
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
Problem 1P
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Question
Calculate the standard error of regression (SER) for the Lineweaver–Burk slope and the Eadie–Hofstee slope to compare the precision of each.
please answer this question
Eadie–Hofstee SER:
it is not 0.128, 0.028, 0.136, or 0.1362.
![A kinetic study of an intestinal peptidase using glycylglycine as the substrate produced the experimental data shown in the table.
glycylglycine + H₂O → 2 glycine
[S] (MM)
1.5
2.0
3.0
4.0
8.0
16.0
Calculate the standard error of regression (SER) for the Lineweaver-Burk slope and the Eadie-Hofstee slope to compare the
precision of each.
Product formed (µmol min-¹)
0.21
0.24
0.28
0.33
0.40
0.45
Lineweaver-Burk SER: 0.182
Eadie Hofstee SER:
0.128
Incorrect
μmol min
μmol min
-1](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F51044012-1e7d-4f53-9311-c2b96c730020%2F73556892-2abc-4463-ba63-432442a9c3eb%2F0m6uita_processed.jpeg&w=3840&q=75)
Transcribed Image Text:A kinetic study of an intestinal peptidase using glycylglycine as the substrate produced the experimental data shown in the table.
glycylglycine + H₂O → 2 glycine
[S] (MM)
1.5
2.0
3.0
4.0
8.0
16.0
Calculate the standard error of regression (SER) for the Lineweaver-Burk slope and the Eadie-Hofstee slope to compare the
precision of each.
Product formed (µmol min-¹)
0.21
0.24
0.28
0.33
0.40
0.45
Lineweaver-Burk SER: 0.182
Eadie Hofstee SER:
0.128
Incorrect
μmol min
μmol min
-1
![There are several ways to transform the Michaelis-Menten
equation so as to plot data and derive kinetic parameters, each
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.
Vo = -(Km)
[S]
+ Vmax
Vo
Consider the plot of Vo versus for an enzyme-catalyzed
[S]
reaction. The control reactions (blue curve) did not contain
any inhibitor.
curve B
curve C
curve A
V₁
V mas
A
B
Slope =-K
V₁
[S]
Which of the other curves (A, B, or C) depicts this enzyme's activity in the presence of a competitive inhibitor?
C
J
mak
K
m](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F51044012-1e7d-4f53-9311-c2b96c730020%2F73556892-2abc-4463-ba63-432442a9c3eb%2Fotmex0f_processed.jpeg&w=3840&q=75)
Transcribed Image Text:There are several ways to transform the Michaelis-Menten
equation so as to plot data and derive kinetic parameters, each
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.
Vo = -(Km)
[S]
+ Vmax
Vo
Consider the plot of Vo versus for an enzyme-catalyzed
[S]
reaction. The control reactions (blue curve) did not contain
any inhibitor.
curve B
curve C
curve A
V₁
V mas
A
B
Slope =-K
V₁
[S]
Which of the other curves (A, B, or C) depicts this enzyme's activity in the presence of a competitive inhibitor?
C
J
mak
K
m
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