Abstract
Extracts of total human adipose tissue are able to hydrolyze in vitro cholesterol [ 14C]oleate. The adipocytes are shown to contain most (if not all) of this catalytic activity. Under the experimental conditions, enzymic hydrolysis is maximum at pH 6.0 ± 0.2 and requires the presence of bovine serum albumin. It is markedly inhibited by various surfactants. The results obtained suggest that this sterol monoester lipase activity is distinct from the monoglyceride lipase of adipose tissue active towards monoglycerides and esters of fatty acids and short-chain normal primary alcohols.
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