Abstract
Arginase from the gills of the bivalve Semele solida was inactivated by diethyl pyrocarbonate (DEPC) in a pseudo-first-order reaction with a bimolecular rate constant of 160 M −1 min −1. The reaction order with respect to DEPC concentration was ∼1, the inactivation followed a titration curve for a residue with a pK a of 6.4 at 25°C and the enzymatic activity was restored by hydroxylamine. It is concluded that inactivation results from the modification of a single histidine residue. Borate, a noncompetitive inhibitor with respect to arginine, protected the enzyme from inactivation by DEPC.
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