1975•Canadian Journal of BiochemistryRequires access

Porcine Chymotrypsin A-π, a More Acidic Chymotrypsin

Eveline de Médicis, Louise Bergeron

Abstract

A kinetic study of procine chymotrypsin A-pi revealed two characteristic properties of this type of chymotrypsin: 1. Porcine chymotrypsin A-pi, like bovine chymotrypsin B-pi does not bind proflavin, which is a competitive inhibitor of bovine trypsin and chymotrypsin A-alpha. 2. The pH profiles of the steady-state parameters show the two usual important pK's. The basic one, pK2 = 9.6, affects both Km and kcat/Km and probably controls the binding conformation of chymotrypsin. The acidic one, pK1 = 5.7, affects kcat and kcat/Km and plays a role in the catalytic process. The value of pK1 is unusually low.

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Key concepts: Chymotrypsin, Chemistry, Trypsin, Kinetics, Enzyme, Stereochemistry, Biochemistry, Physics