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glycylglycine + H₂O [S] (MM) 1.5 2.0 3.0 10 using gly 2 glycine Product formed (μmol min¹¹) 0.21 0.24 0.28 000 tab

glycylglycine + H₂O [S] (MM) 1.5 2.0 3.0 10 using gly 2 glycine Product formed (μmol min¹¹) 0.21 0.24 0.28 000 tab

Chemistry
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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Please answer the last question 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
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
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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