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I. Structural analogs of typical substrates of alpha-chymotrypsin. II. 1-acetyl-2-[L-tyrosyl] hydrazine : an inhibitor of alpha-chymotrypsin. III. Binuclear aromatics as inhibitors of alpha-chymotrypsin-catalyzed hydrolyses. IV. Applicability of the pH-stat to alpha-chymotrypsin-catalyzed hydrolyses that produce a buffer

Citation

Kurtz, Abraham Nathan (1960) I. Structural analogs of typical substrates of alpha-chymotrypsin. II. 1-acetyl-2-[L-tyrosyl] hydrazine : an inhibitor of alpha-chymotrypsin. III. Binuclear aromatics as inhibitors of alpha-chymotrypsin-catalyzed hydrolyses. IV. Applicability of the pH-stat to alpha-chymotrypsin-catalyzed hydrolyses that produce a buffer. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechETD:etd-06302006-085322

Abstract

Substitution of a nitrogen atom in place of the C-H group that occurs at the asymmetric center of typical substrates of alpha-chymotrypsin results in the complete loss of the ability of the enzyme to catalyze the hydrolysis of the carboethoxy or carboxamido group. However, the nitrogen-substituted analogs, which otherwise possess all of the remaining significant structural entities of typical substrates, function as inhibitors of alpha-chymotrypsin catalyzed hydrolyses but in general show less affinity for the enzyme than do the analogous C-H containing substrates.

It has been found that l-acetyl-2-[L-tyrosyl] hydrazine is a reversible inhibitor of alpha-chymotrypsin catalyzed hydrolyses with unusual affinity for the enzyme. At pH 7.9 the enzyme inhibitor constant was found to have a value of KI = 0.074 x 10(-3)M, which shows that this substance associates reversibly with alpha-chymotrypsin at the active site to a greater extent than any other known substrate or reversible inhibitor.

Preliminary results, based upon inhibition studies, indicate that alpha-chymotrypsin possesses a greater affinity for the naphthalene function than for the indole function.

A study of the applicability of the pH-stat to alpha-chymotrypsin catalyzed hydrolyses that produce a buffer showed that the reliability was a function of the buffer capacity. Amides gave poor results; hydrazides gave good or fair results, one of which contradicted a literature value, and a hydroxamide gave excellent results.

Item Type:Thesis (Dissertation (Ph.D.))
Degree Grantor:California Institute of Technology
Division:Chemistry and Chemical Engineering
Major Option:Chemistry
Thesis Availability:Public (worldwide access)
Research Advisor(s):
  • Niemann, Carl G.
Thesis Committee:
  • Unknown, Unknown
Defense Date:1 January 1960
Record Number:CaltechETD:etd-06302006-085322
Persistent URL:http://resolver.caltech.edu/CaltechETD:etd-06302006-085322
Default Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:2789
Collection:CaltechTHESIS
Deposited By: Imported from ETD-db
Deposited On:14 Jul 2006
Last Modified:26 Dec 2012 02:54

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