I. The alpha-chymotrypsin-catalyzed and base-catalyzed hydrolysis of some substituted glycine esters and related compounds. II. The nature and properties of the enzyme-substrate complex produced under conditions of very high substrate concentrations. III. A hypothesis concerning alpha-chymotrypsin-substrate complexes

Citation

Wolf, John P. (1959) I. The alpha-chymotrypsin-catalyzed and base-catalyzed hydrolysis of some substituted glycine esters and related compounds. II. The nature and properties of the enzyme-substrate complex produced under conditions of very high substrate concentrations. III. A hypothesis concerning alpha-chymotrypsin-substrate complexes. Dissertation (Ph.D.), California Institute of Technology. doi:10.7907/KPJF-0G56. https://resolver.caltech.edu/CaltechETD:etd-02212006-134559

Abstract

A series of substituted glycogen esters have been evaluated as substrates for [alpha]-chymotrypsin. The second order base-catalyzed hydrolysis constants for these compounds have also been determined.

Four substrates for [alpha]-chymotrypsin have been found to exhibit unusual kinetic behavior at very high concentrations in the presence of [alpha]-chymotrypsin. It has been shown that these data can be the result of two molecules of substrate combining with each enzyme active site.

A hypothesis concerning the enzyme-substrate complex is offered which helps to correlate the data given in this work.

Thesis Files