Abstract
The aim of this work was to test the specificity of rat liver cholesterol esterase (sterol-ester hydrolase, EC 3.1.1.13) with regard to the hydrolysis of cis and trans unsaturated cholesterol esters. Several synthetic cholesterol esters were employed as model substrates for the soluble fraction and microsomes from rat liver homogenates. In all cases, trans fatty acid cholesterol esters were hydrolyzed to a lesser degree than cis unsaturated esters. Furthermore, a preference for the 9- cis-unsaturated octadecanoates was indicated. The ability of cholesterol esterase to recognize the shape of the acyl moiety of cholesterol esters is discussed.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
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