Parification and properties of acylase from Ehrlich ascites carcinoma cells.

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Abstract
The acylase of Ehrlich ascites carcinoma cells was purified by fractionation with ammonium sulfate, diethylaminoethyl cellulose chromatography, Sephadex. G-200 gel filtration, and hydroxylapatite chromatography. The acylase activity of the purified enzyme toward N-dichloroacetyl-L-aspartic acid was 1561 U/mg and it was represented about 410 fold purification over the cell free extract. The enzyme has a pH optimum around 8.5 toward N-dichloroacetyl-L-aspartic acid. It is inhibited by Sn2+, Mn2+, Cu2+, Hg2+, Zn2+, p-chloromercuribenzoate, ICH2COOH, H2O2, and diisopropyl fluorophosphate. As a result of the investigation of substrate specificity, it was found that the enzyme hydrolyzed only N-dichloroacetyl-L-aspartic acid among eleven kinds of N-dichloroacetyl amino acids. But it could not hydrolyze D from of N-dichloroacetyl-aspartic acid. In order to test the effect of acyl groups toward the enzyme activity, eleven acyl aspartic acids were tested. N-Chloroacetyl, N-dichloroacetyl, N-trifluoroacetyl derivatives of L-aspartic acid were hydrolyzed.

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