CHARACTERIZATION OF ENZYMES HYDROLYZING ACYL NAPHTHYLAMIDES: II. TRIHALOGEN DERIVATIVES

Abstract

Enzymes in guinea pig homogenates hydrolyzing a variety of halogenated and nonhalogenated acyl α- and β-naphthylamide substrates can be separated into two major groups on the basis of substrate hydrolysis rates, solubility and affector characteristics. Both groups of enzymes, those acting on the non-, mono- and dihalogenated acyl naphthylamides and those acting on trihalogen derivatives, have characteristics like those of arylesterases and are inseparable from enzymes hydrolyzing naphthol AS acetate. These enzymes are, However, separable on fractionation by starch gel electrophoresis and DEAE-cellulose chromatography from several enzymes catalyzing the hydrolysis of N-acyl amino acids (acylase I and II) and several amino acid β-naphthylamides. Species differences exist in the characteristics of enzymic hydrolysis of these acylarylamides.