Substrate specificity of carboxylesterase (E.C.3.1.1.1) from several animals.

Publisher Website
Google Scholar
Abstract
The substrate specificity of purified esterase from various origins using p-nitrophenyl acetate, .alpha.-naphthyl acetate and trans-4-aminomethylcyclohexanecarboxylic acid esters as substrates. Attention was focused on the influence of structural properties of trans-4-aminomethylcyclohexanecarboxylic acid esters. The hydrolysis rate of .alpha.-naphthyl acetate of p-nitrophenyl acetate differed markedly according to animal species. In all the enzymes from rats, guinea pigs, rabbits and pigs, phenyl ester was hydrolyzed more readily than benzyl ester or alkyl ester. The hydrolysis rate of phenyl esters was affected by the steric as well as electronic effect of the substituents.

This publication has 1 reference indexed in Scilit: