Variation of the Conformation of the Active Site of α-Chymotrypsin: I. Hydrogen Ion Concentration Studies. II. Electrolyte Concentration Studies

Author: Mukatis, Werner Alfred

Year: 1965

Degree: Dissertation (Ph.D.)

Advisor: Niemann, Carl G.

Committee Member: Unknown, Unknown

Option: Chemistry

DOI: 10.7907/SZB4-EM75

Abstract

NOTE: Text or symbols not renderable in plain ASCII are indicated by [...]. Abstract is included in .pdf document.

The initial velocities of [alpha]-chymotrypsin-catalyzed hydrolyses of acylated amino acid esters follow the rate law [...] when the only variables are initial substrate and enzyme concentration. In the above equation, [...] is the initial velocity, [...] and [...] are initial enzyme and substrate concentration, respectively, and [...] and [...] are a pair of experimentally determined kinetic parameters. Factors such as temperature, ionic strength, hydrogen-ion concentration, structure of substrate, etc., affect the values of [...] and [...].

Variation in the kinetic parameters [...],[...], and [...] for selected substrates and variations in the ratios of the parameters [...],[...]and [...] for selected pairs of substrates are studied as functions of hydrogen-ion concentration and concentration of added electrolyte.

The results are discussed in terms of possible changes in conformation of the active site of [alpha]-chymotrypsin with changing hydrogenion concentration and concentration of added electrolyte.

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