Abstract
The properties of aortic cholesterol esterase have been examined in subcellular fractions of rat and monkey aortic homogenates. Hydrolysis of a variety of labeled cholesteryl esters added as an acetone solution was demonstrated in both microsomal and high speed supernatant fractions. Cholesteryl oleate and linoleate were hydrolyzed to a greater extent than cholesteryl palmitate and stearate. A broad pH optimum for enzyme activity was observed in both the high speed supernatant and microsomal fractions. Product inhibition with cholesterol was not apparent although fatty acids added to the system reduced cholesterol esterase activity. The mode of substrate introduction was found to be an important factor in determining the extent of enzymatic activity. Studies on the sequence of substrate addition suggested that substrate introduced in acetone did not equilibrate with endogenous cholesteryl ester. Preincubation of the enzyme solution or addition of bile salt did not affect hydrolytic activity. No significant difference in cholesterol esterase activity was apparent between control and atherosclerotic monkey aorta.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
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