Abstract
Lysosomal cholesterol esterase from rabbit liver was solubilized with digitonin and purified 21, 000-fold to homogeneity by Bio-Gel A-1.5m, DEAE-Bio-Gel A, Phenyl-Sepharose column chromatography, preparative slab gel electrophoresis and finally Sephacryl S-200 column chromatography. The molecular weight of the purified enzyme, calculated by SDS-polyacrylamide gel electropholesis, was about 42, 000. The enzyme hydrolyzed both cholesterol oleate and triolein. It was activated by phospholipids (phosphatidylcholine, phosphatidylethanolamine) and lysosomal membrane. The enzyme was adsorbed on Phenyl-Sepharose and Concanavalin A-Sepharose anddissociated from them by ethylene glycol and a-methylmannoside, respectively, suggesting that it was a hydrophobic glycoprotein. We also discuss the implication of the enzyme for the accumulation of cholesterol ester in atheromatous aorta.
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