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 or 0.013.
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 or 0.013.
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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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 or 0.013.
![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%2F4ddf98fc-9210-4350-a193-fc3d4b94a6b7%2Fsh4xvmr_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
![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%2F4ddf98fc-9210-4350-a193-fc3d4b94a6b7%2Fwwjw8w9_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
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