A new automated method for phenotyping arylesterase (EC 3.1.1.2) based upon inhibition of enzymatic hydrolysis of 4-nitrophenyl acetate by phenyl acetate.
A new method for phenotyping human serum arylesterase (EC 3.1.1.2) is described and evaluated. The aromatic esters, phenyl acetate and 4-nitrophenyl acetate, were compared as substrates for spectrophotometric measurement of arylesterase activity. A method for arylesterase phenotyping, based upon inhibition of the enzymatic hydrolysis of 4-nitrophenyl acetate by phenyl acetate, was developed. The method was applied to serum samples from 158 blood donors and showed a distinct separation of the three phenotypes defined by a reference method based on the ratio of paraoxonase activity to arylesterase activity using paraoxon and phenyl acetate as substrates. The method was adapted to a Cobas-Fara centrifugal analyser.
Haagen
L
L
University of Aarhus, Department of Clinical Chemistry, Randers Centralsygehus, Denmark.
Brock
A
A
D000483:Alleles; D001782:Blood Donors; D002265:Carboxylic Ester Hydrolases / Q000097:blood* / Q000235:genetics; D006801:Humans; D006868:Hydrolysis; D007527:Isoenzymes / Q000097:blood* / Q000235:genetics; D007700:Kinetics; D009596:Nitrophenols / Q000737:chemistry*; D010641:Phenotype; D010648:Phenylacetates / Q000737:chemistry*; D013379:Substrate Specificity
D007527:Isoenzymes; D009596:Nitrophenols; D010648:Phenylacetates; C008642:4-nitrophenyl acetate; D002265:Carboxylic Ester Hydrolases; C019734:arylesterase; C025136:phenylacetic acid