Author Type

Graduate Student

Date of Award

1972

Document Type

Thesis

Publication Status

Version of Record

Submission Date

October 2026

Abstract

The effects of added salt on the deacylation rate constant of trans-cinnamoylchymotrypsin were examined. Ionic strength effects on the equilibrium constant of an ionizable, enzymic group of pKa 7.25 were also studied. Through the development of methods for the precise measurement of pH and observed rate constants, very small changes in the experimental parameters could be detected. It was found that neither the deacylation rate constant nor the kinetically determined pKa exhibited a significant salt effect over the ionic strength range of 0.04 to 0.12 M. Based on the known three-dimensional structure of the active site of chymotrypsin, four plausible mechanisms were considered in light of the experimental absence of salt effects. The presence of calcium ion at low concentrations significantly perturbed the values of the deacylation rate constant and the protonic equilibrium constant.

Extent

83 p.

Comments

Thesis (M.S.)--Florida Atlantic University, 1972.|Charles E. Schmidt College of Science|FAU Electronic Theses and Dissertations Collection|Thesis (M.S.)--Florida Atlantic University, 1972.

Identifier

FADT13496

Format

pdf

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