Porcine Chymotrypsin A-π, a More Acidic Chymotrypsin
Copyright policy )Porcine Chymotrypsin A-π, a More Acidic Chymotrypsin
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, 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.
Kinetics, Swine, Flavins, Animals, Chymotrypsin, Tyrosine, Hydrogen-Ion Concentration, Protein Binding
Kinetics, Swine, Flavins, Animals, Chymotrypsin, Tyrosine, Hydrogen-Ion Concentration, Protein Binding
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