Physicochemical Properties of the Long‐Chain‐Acyl‐CoA Hydrolase from Rat Liver Microsomes

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Abstract
The physicochemical properties of a long-chain-acyl-CoA hydrolase (EC 3.1.2.2) of rat liver microsomes were studied. The hydrolase sedimented as a homogenous species with a sedimentation coefficient, s20,w, of 4.1 S and the MW of 59,000 was obtained. Amino acid composition of the enzyme was determined. The specific absorption coefficient, .**GRAPHIC**. was estimated as 9.8 (1 cm cell length) and the circular dichroic data suggested 50-60% .alpha.-helical structure. The enzyme contained 3 sulfydryl groups, and 1 of these was exposed to the environment. The hydrolase was inhibited by the serine-directed reagent phenylmethylsulfonyl fluoride, as well as p-hydroxymercuribenzoate, N-ethylmaleimide and 5,5''-dithiobis(2-nitrobenzoic acid). Reactivation by dithiothreitol was never complete with phenylmethylsulfonyl fluoride and p-hydroxymercuribenzoate as inhibitors.