Porcine Chymotrypsin A-π, a More Acidic Chymotrypsin

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Abstract

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

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