CYTOSOLIC CHOLESTEROL ESTER HYDROLASE FROM BOVINE CORPUS-LUTEUM - ITS PURIFICATION, IDENTIFICATION, AND RELATIONSHIP TO HORMONE-SENSITIVE LIPASE
CYTOSOLIC CHOLESTEROL ESTER HYDROLASE FROM BOVINE CORPUS-LUTEUM - ITS PURIFICATION, IDENTIFICATION, AND RELATIONSHIP TO HORMONE-SENSITIVE LIPASE
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DOI：
10.1016/0005-2760(83)90231-x
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发表时间：
1983-01-01
期刊：
影响因子：
--
通讯作者：
YEAMAN, SJ
中科院分区：
文献类型：
--
作者：
COOK, KG;COLBRAN, RJ;YEAMAN, SJ
The cytosolic cholesterol ester hydrolase from bovine corpus luteum was purified 760-fold, using isoelectric precipitation and gel filtration chromatography, followed by ion-exchange and adsorption chromatographies in the presence of non-ionic detergent. Further purification was achieved by affinity chromatography on triacylglycerol-containing polyacrylamide-agarose. The partially purified enzyme was inhibited by NaF, HgCl2 and DFP. Incubation with [3H]DFP resulted in specific labeling of a polypeptide of MW = 84,000, the same subunit MW as that of the enzyme from adrenal cortex. This MW 84,000 polypeptide was phosphorylated by the catalytic subunit of cAMP-dependent protein kinase, phosphorylation causing greater than 2-fold activation of the enzyme. Several properties of the cholesterol ester hydrolase from corpus luteum show striking similarities to those of hormone-sensitive lipase from adipose tissue. This provides further evidence that hormone-sensitive lipase, in addition to its role in adipose tissue lipolysis, has a key role in steroidogenic tissues, namely catalyzing the supply of free cholesterol from the cholesterol ester stores.
