Accession Number : AD0723229

Title :   Characterization of the Esterases of Canine Serum,

Corporate Author : DALHOUSIE UNIV HALIFAX (NOVA SCOTIA) DEPT OF PHARMACOLOGY

Personal Author(s) : Ecobichon,D. J.

Report Date : 19 JUN 1970

Pagination or Media Count : 10

Abstract : Various techniques including electrophoresis, gel filtration, and titrimetric and spectrophotometric analysis with specific and nonspecific substrates and inhibitors were used to characterize the serum esterases of male and female dogs. Electrophoresis in starch gel yielded 10 distinct bands of activity: four butyrylcholinesterase bands, an esterolytically active albumin, and five bands of aliesterase and/or arylesterase activity. Gel filtration on Sephadex G-200 yielded two distinct peaks of activity, one containing the cholinesterase bands, and the second peak containing both arylesterase and aliesterase activity in close association with the serum albumin. Kinetic characteristics determined for the canine serum esterases included (1) optimal pH; (2) Km values for esters of choline, alpha-naphthol, and p-nitrophenol; and (3) average rates of hydrolysis of alpha-naphthyl acetate, butyrylcholine iodide, p-nitrophenyl acetate, and E600 by the sera of males and females. The sensitivity of the serum esterases to inhibition by various cations, and specific and nonspecific inhibitors was investigated. The organophosphate, E600, may be a highly specific substrate for the detection and quantification of arylesterase in a mixture of nonspecific carboxylesterases. (Author)

Descriptors :   (*CARBOXYLIC ESTER HYDROLASES, *DOGS), (*BLOOD SERUM, DOGS), (*ENZYMES, DOGS), CHEMICAL ANALYSIS, ELECTROPHORESIS, CANADA

Subject Categories : Biochemistry

Distribution Statement : APPROVED FOR PUBLIC RELEASE