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Unformatted text preview: In contrast, it is harder to
determine the decrease in reactants with high accuracy because you may be required to measure what
could be just a small decrease in a relatively large starting value. So, all things being equal, most
enzymologists measure the rate of product formation, if at all possible.
Question 2: You have collected experimental data that show that an enzyme you are studying follows the kinetic
scheme below. [Hint: Recall the assumptions that underlie the steady-state approximation and are the basis of the
Michaelis-Menten treatment of enzyme-catalyzed reactions.]
where k1 = 10 M s ; k2 = 10 s ; k3 = 10 s ; and, k4 = 10 M s ....
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This note was uploaded on 03/15/2014 for the course MCB 102 taught by Professor Staff during the Fall '08 term at University of California, Berkeley.
- Fall '08