Small C A, Yeaman S J, West D W, Clegg R A
Department of Biochemistry and Genetics, University of Newcastle upon Tyne, U.K.
Biochim Biophys Acta. 1991 Apr 3;1082(3):251-4. doi: 10.1016/0005-2760(91)90200-2.
Neutral cholesterol esterase activity is expressed in extracts of mammary epithelial cells. The identity of the enzyme catalyzing this hydrolysis was investigated. Anti-hormone-sensitive lipase immunoglobulin elicited the total inhibition of this activity and also immunoprecipitated a single phosphoprotein of Mr 84 kDa from mammary cell extracts previously phosphorylated in vitro with [gamma-32P]ATP and cyclic AMP-dependent protein kinase. It is concluded that mammary cell cholesterol esterase activity results from the presence of hormone-sensitive lipase.
中性胆固醇酯酶活性在乳腺上皮细胞提取物中得以表达。对催化这种水解作用的酶的特性进行了研究。抗激素敏感性脂肪酶免疫球蛋白可使该活性完全受到抑制，并且还能从先前用[γ-32P]ATP和环磷酸腺苷依赖性蛋白激酶在体外进行磷酸化处理的乳腺细胞提取物中免疫沉淀出一种分子量为84 kDa的单一磷蛋白。得出的结论是，乳腺细胞胆固醇酯酶活性源于激素敏感性脂肪酶的存在。
