title: Human red cell butyrylesterase, and its homologies in thirteen other mammalian species.
abstract: The selective staining of a single butyrylesterase, following isoelectric focusing of red cell lysates from 14 mammalian species, including man, was achieved using the chromogenic substrate N-acetyl-L-alanine-alpha-naphthyl ester. This procedure optimized the identification of this enzyme, and a close correspondence of its properties was observed in all the species investigated. The inhibition profile, using a range of inhibitors, was identical in all cases. Particularly noteworthy was the activation of the enzyme by p-chloromercuribenzoate at low (2-20 x 10(-6) M) concentrations, but inhibition at higher (greater than 10(-3) M) concentrations. The isoelectric points of all samples fell within a narrow range, pI 4.00-4.43. Descriptions of this activity in different animals, under different designations, could be identified in earlier studies, and the enzyme was uniformly designated "butyrylesterase 1". A tetrameric subunit structure, previously established for the human enzyme, was also demonstrated in the case of mouse butyrylesterase 1. A list of diagnostic characteristics for the enzyme was presented, and it was assumed that the 14 enzymes investigated are orthologous. It was not possible to group butyrylesterase 1 with any other known esterase within the system of enzymes recommended by the IUB, and it was proposed that this enzyme be assigned to a new esterase subclass.
mesh_terms: D000818:Animals; D002265:Carboxylic Ester Hydrolases / Q000097:blood*; D002415:Cats; D002417:Cattle; D002729:Chloromercuribenzoates / Q000494:pharmacology; D004285:Dogs; D004789:Enzyme Activation; D004912:Erythrocytes / Q000201:enzymology*; D005849:Gerbillinae; D006041:Goats; D006168:Guinea Pigs; D006736:Horses; D006801:Humans; D007525:Isoelectric Focusing; D051379:Mice; D011817:Rabbits; D051381:Rats; D012756:Sheep; D013552:Swine
chemical_list: D002729:Chloromercuribenzoates; D002265:Carboxylic Ester Hydrolases; C021487:butyrylesterase