BIOC12H3 Lecture Notes - Lecture 8: Enzyme Kinetics, Enzyme Inhibitor, Enzyme

90 views7 pages
30 Sep 2012
School
Course

Document Summary

Measurement of km and vmax: double-reciprocal (lineweaver-burk) plot to determine vmax and km. The michaelis menten equation can be rewritten in order to obtain values for vmax and. The most commonly used transformation is the double- reciprocal, or lineweaver burk, plot in which the values of 1/v0 are plotted against 1/[s] (figure 5. 6 slide 2). The absolute value of 1/km is obtained from the intercept of the line at the x axis, and the value of 1/vmax is obtained from the y intercept. Although double-reciprocal plots are not the most accurate methods for determining kinetic constants, they are easily understood and provide recognizable patterns for the study of enzyme inhibition. Values of kcat can be obtained from measurements of vmax only when the absolute concentration of the enzyme is known. Values of km can be determined even when enzymes have not been purified provided that only one enzyme in the impure preparation can catalyze the observed reaction.

Get access

Grade+20% off
$8 USD/m$10 USD/m
Billed $96 USD annually
Grade+
Homework Help
Study Guides
Textbook Solutions
Class Notes
Textbook Notes
Booster Class
40 Verified Answers
Class+
$8 USD/m
Billed $96 USD annually
Class+
Homework Help
Study Guides
Textbook Solutions
Class Notes
Textbook Notes
Booster Class
30 Verified Answers

Related Documents

Related Questions