Clinical Chemistry
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Clinical Chemistry 24: 1177-1181, 1978;
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Clinical Chemistry, Vol 24, 1177-1181, Copyright © 1978 by American Association for Clinical Chemistry

Biochemical characterization of an aryl acetic ester hydrolase isolated from human monocytes

WK Lam, E Taft and LT Yam

A carboxylic-ester hydrolase was isolated from the leukocytes of a patient with myelomonocytic leukemia. Its relative molecular mass as estimated by sucrose density-gradient sedimentation is about 70 000. The purified enzyme is specific for acetyl esters of aromatic alcohols. It is inhibited by fluoride, but insensitive to eserine or p- chloromercuriphenylsulfonate. Hydrolysis of 1-naphthyl acetate was optimal above pH 6.0; of o-nitrophenyl acetate, above 8.0. The common catalytic site for the two types of substrates on the enzyme was confirmed by competitive inhibition data.




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Copyright © 1978 by the American Association for Clinical Chemistry.