The characterization and assay of enzymes in rat adrenal cortex. 1. Esterase and phosphatase activities

Abstract

Homogenates of demedullated rat adrenals showed greater esterase activity with triacetin and tributyrin than with aliphatic esters of primary alcohols, and were inactive towards triolein. Choline esters were hydrolysed much less readily than tributyrin. Bile salts and CUSO4 inhibited the aliphatic esterase. Eserine, Nu 683, (the dimethylcarbamate of 2-hydroxy-5-phemylbenzyl-trimethylammonium bromide), and 2987 R. P. (N-diethylaminoethyl phenothiazine) but not Nu 1250 (N-p-chlorophenyl-N-methylcarbamate of m-hydroxyphenyltri-methylammonium bromide), inhibited the cholinesterase. The phosphomonoesterase, pyrophosphatase and adenosinetriphosphatase activities of such homogenates were also studied. Acid phosphatase was inhibited by CUSO4, formaldehyde, ethanol and DL-tartrate, but not by FeSO4.