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- W2065979467 abstract "Hydrolysis of 1-palmitoyl-2-linoleoyl-phosphatidylcholine (PLPC) hydroperoxide (PLPC-OOH) in PLPC liposomal membrane by Crotalus adamanteus venom phospholipase A2 (PLA2) was studied by measuring the decay of PLPC and PLPC-OOH and the formation of linoleate and linoleate hydroperoxide. We demonstrate that PLA2 has a preference to hydrolyze PLPC-OOH over PLPC when more than 25 mole % of cholesterol is incorporated into the PLPC liposomal membrane. Similar results were obtained for PLPC hydroxide (PLPC-OH). These results suggest that cholesterol displaces the hydrophilic hydroperoxyl and hydroxyl moieties of PLPC-O(O)H to the surface interface of the liposomal membrane where they are more accessible to PLA2 hydrolysis." @default.
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- W2065979467 date "1998-04-01" @default.
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- W2065979467 title "Preferential Hydrolysis of Oxidized Phosphatidylcholine in Cholesterol-Containing Phosphatidylcholine Liposome by Phospholipase A2" @default.
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- W2065979467 doi "https://doi.org/10.1006/bbrc.1998.8421" @default.
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