Publication Date

1972

Document Type

Dissertation/Thesis

First Advisor

Marshall, Thomas H. (Professor of chemistry)||Kevill, Dennis N.||Erman, James E.

Degree Name

M.S. (Master of Science)

Department

Department of Chemistry

LCSH

Chymotrypsin||Enzymes||Elastases

Abstract

The p-nitrophenyl esters of a homologous series of straight chain fatty acids were used as substrates for elastase and chymotrypsin. As the straight chain length increases, the deacylation rate of the acyl-enzyme increases regularly to a maximum and then declines. Examination of the activation parameters reveals that the degree of specificity results from enthalpy control rather than entropy. This appears to contradict, in varying degrees, the results of three previously published studies of chymotrypsin deacylation. Arguments are presented that some of the discrepancy can be explained in terms of different experimental methods being used and a detailed examination of the deacylation process in light of current theories of protein conformation. Elastase catalyzed hydrolysis of p-nitrophenyl N-benzyloxycarbonyl glycinate (CBZ-Gly-pNPE) and p-nitrophenyl t-butyloxycarbonyl-L-alaninate (NBA) are studied. The heat of ionization of the essential group in the active site of elastase, presumably histidine, is measured and discussed.

Comments

Includes bibliographical references.||Includes illustrations.

Extent

55 pages

Language

eng

Publisher

Northern Illinois University

Rights Statement

In Copyright

Rights Statement 2

NIU theses are protected by copyright. They may be viewed from Huskie Commons for any purpose, but reproduction or distribution in any format is prohibited without the written permission of the authors.

Media Type

Text

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