title: Nonserine esterases from rat liver cytosol.
abstract: An effort to identify the major general esterases of rat liver cytosol that are insensitive to the serine esterase inhibitor paraoxon (diethyl 4-nitrophenyl phosphate) has led to the isolation of a dozen enzymes. Four of these are electrophoretically homogeneous. Although purified on the basis of their hydrolytic activity toward 4-nitrophenyl acetate, each of the enzymes has a very broad and overlapping substrate specificity for aromatic esters. Thiol esters serve as substrates but, within the limits of the methods used, amides are not hydrolyzed.
authors: Laboratory of Biochemistry and Metabolism, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892.
authors: D H
authors: DH
authors: Kim
authors: Y S
authors: YS
authors: Yang
authors: W B
authors: WB
authors: Jakoby
mesh_terms: D000818:Animals; D002845:Chromatography / Q000379:methods; D003600:Cytosol / Q000201:enzymology; D004950:Esterases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D008970:Molecular Weight; D010261:Paraoxon; D051381:Rats; D013379:Substrate Specificity
chemical_list: D004950:Esterases; D010261:Paraoxon