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

Citation

Mukatis, Werner Alfred (1965) Variation of the Conformation of the Active Site of α-Chymotrypsin: I. Hydrogen Ion Concentration Studies. II. Electrolyte Concentration Studies. Dissertation (Ph.D.), California Institute of Technology. doi:10.7907/SZB4-EM75. https://resolver.caltech.edu/CaltechETD:etd-01232004-141835

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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