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

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 a...

Full description

Bibliographic Details
Main Author: Kurtz, Abraham Nathan
Format: Others
Published: 1960
Online Access:https://thesis.library.caltech.edu/2789/1/Kurtz_an_1960.pdf
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. doi:10.7907/8C7N-4Z18. https://resolver.caltech.edu/CaltechETD:etd-06302006-085322 <https://resolver.caltech.edu/CaltechETD:etd-06302006-085322>