Biochemical characterization of an aryl acetic ester hydrolase isolated from human monocytes.
Open Access
- 1 July 1978
- journal article
- research article
- Published by Oxford University Press (OUP) in Clinical Chemistry
- Vol. 24 (7) , 1177-1181
- https://doi.org/10.1093/clinchem/24.7.1177
Abstract
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.This publication has 5 references indexed in Scilit:
- A Method for Determining the Sedimentation Behavior of Enzymes: Application to Protein MixturesJournal of Biological Chemistry, 1961
- Fractionation of C-esterase from the hog's kidney extractBiochemical Journal, 1960
- CHLOROACYL ESTERS AS HISTOCHEMICAL SUBSTRATESJournal of Histochemistry & Cytochemistry, 1953
- The determination of enzyme inhibitor constantsBiochemical Journal, 1953
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951