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I. The consequences of systematic error in enzyme kinetics. II. L-tyrosyl-L-tyrosine derivatives for the detection of transpeptidation in alpha-chymotrypsin-catalyzed hydrolyses. III. The interaction of alpha-methyl-alpha-acylamino acids with alpha-chymotrypsin. IV. The apparent ionization constants of a series of phenylalanine derivatives

Citation

Almond, Harold Russell (1961) I. The consequences of systematic error in enzyme kinetics. II. L-tyrosyl-L-tyrosine derivatives for the detection of transpeptidation in alpha-chymotrypsin-catalyzed hydrolyses. III. The interaction of alpha-methyl-alpha-acylamino acids with alpha-chymotrypsin. IV. The apparent ionization constants of a series of phenylalanine derivatives. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechETD:etd-03272006-084330

Abstract

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The consequences of systematic error in enzyme kinetics were investigated. Systematic error in substrate blank, enzyme blank, velocity determination, substrate concentration and the Beer-Lambert relationship was considered. The advisability of using weighting procedures in the presence of systematic error was questioned.

L-Tyrosyl-L-tyrosine methyl ester, amide, hydrazide and hydroxamide were prepared in order to detect transpeptidation in alpha-chymotrypsin-catalyzed hydrolyses. The reaction products from the hydrolyses of the corresponding L-tyrosine derivatives were found to contain only negligible amounts of transpeptidation products except for L-tyrosinhydroxamide which gave some L-tyrosyl-L-tyrosine. alpha- and beta-chymotrypsin were qualitatively the same with respect to these reactions.

The N-acetyl methyl esters of alpha-methylphenylalanine, alpha-methyltyrosine and alpha-methyl-beta-(2-naphthyl)-alanine were synthsized and resolved. These esters are good competitive inhibitors of alpha-chymotrypsin. N-acetyl-(-) alpha-methyl-beta-(2-naphthyl)-alanine is a slowly hydrolyzed substrate of this enzyme. The inactivity of these esters toward alpha-chymotrypsin-catalyzed hydrolysis is a consequence of their inability to react further after complexing with the enzyme.

The [...] values of the alpha-ammonium groups of D,L-phenylalanine amide, thioamide, amidoxime, hydrazide, methyl ester and hydroxamide were determined. Comparison of these [...] values with some for corresponding glycine derivatives shows the former to be 0.59 ± .04 pK units lower. The infrared spectra of these phenylalanine derivatives were determined in KBr.

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 1961
Record Number:CaltechETD:etd-03272006-084330
Persistent URL:http://resolver.caltech.edu/CaltechETD:etd-03272006-084330
Default Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:1164
Collection:CaltechTHESIS
Deposited By: Imported from ETD-db
Deposited On:27 Mar 2006
Last Modified:26 Dec 2012 02:35

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