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  • Title: Catalytic properties of the purified rat hepatic cytosolic cholesteryl ester hydrolase.
    Author: Natarajan R, Ghosh S, Grogan W.
    Journal: Biochem Biophys Res Commun; 1996 Aug 14; 225(2):413-9. PubMed ID: 8753777.
    Abstract:
    The purified enzyme hydrolyzed cholesteryl oleate, cholesteryl linoleate, and triolein at similar rates over a broad range of concentrations. Hydrolytic activity was relatively low with p-nitrophenyl acetate, but much higher with PNP-esters of the more lipophilic C4-C18 fatty acids, in sharp contrast to microsomal esterases which hydrolyze PNP-acetate more efficiently. Zn2+, Cu2+, Cd2+, Hg2+, and phenylmethylsulfonyl fluoride inhibited, whereas N-ethyl maleimide and iodoacetamide stimulated activity of the pure enzyme. Limited trypsin digestion selectively inhibited cholesteryl esterase activity with retention of activity toward PNP-octanoate, suggesting involvement of a trypsin-labile loop in the lipophilic substrate binding pocket.
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