Date of Award:

5-1984

Document Type:

Thesis

Degree Name:

Master of Science (MS)

Department:

Chemistry and Biochemistry

Committee Chair(s)

Elizabeth Boeker

Committee

Elizabeth Boeker

Committee

Jack Spence

Committee

Jack Lancaster

Abstract

The feasibility of using an integrated rate equation to analyze the kinetics of a second-order, enzyme-catalyzed reaction has been investigated. The inducible arginine decarboxylase from Escherichia coli B. was chosen for this study because it catalyzes an irreversible reaction with stoichiometry A --> P + Q, the simplest second order case. Values for five of the eight possible kinetic constants were determined from 21 time courses. Of the remaining three, the uncompetitive product inhibition constant for CO2 was shown to be between 0 and 0.06, while the values of the competitive product inhibition for CO2 and the uncompetitive constant for arginine, agmatine and CO2 simultaneously do not appear to be appreciably different from zero. Initial rate analysis of the time courses gave similar results.

The results obtained by varying the initial agmatine concentration at a low initial arginine concentration were not consistent with the rest of the data. This appears to be due to a fundamental difference in the behavior of the enzyme under those conditions rather than to a problem associated with the analysis.

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0e74d1983b0574ba871470337aa59d90

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