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 O 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.
| Identifer | oai:union.ndltd.org:UTAHS/oai:digitalcommons.usu.edu:etd-8279 |
| Date | 01 May 1984 |
| Creators | Tuttle, Tamra |
| Publisher | DigitalCommons@USU |
| Source Sets | Utah State University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | All Graduate Theses and Dissertations |
| Rights | Copyright for this work is held by the author. Transmission or reproduction of materials protected by copyright beyond that allowed by fair use requires the written permission of the copyright owners. Works not in the public domain cannot be commercially exploited without permission of the copyright owner. Responsibility for any use rests exclusively with the user. For more information contact digitalcommons@usu.edu. |
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