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- W2037974767 abstract "The content of endogenous phospholipids in plasma membrane preparations from Ehrlich ascites cells was depleted by exposure to phospholipase C. The enzyme catalyzing the phosphatidylcholine: ceramide choline phosphotransferase reaction was inactivated by this treatment. However, the activity could be restored with exogenous phosphatidylcholines, demonstrating the dependence of the reaction upon the presence of this substrate. Phosphatidylcholines containing unsaturated fatty acids were 10-fold more effective substrates than the saturated molecular species. The activation energy of the reaction was determined to be 17.2 kcal/mol. Selective trypsin treatment of the plasma membranes suggests that the cholinephosphotransferase may have an asymmetric orientation. The reaction kinetics followed a rate equation similar to that of the ping-pong reaction mechanism, which suggests the formation of an enzyme-bound intermediate of the phosphocholine group being transferred. These results are discussed in terms of possible biological functions of the enzyme." @default.
- W2037974767 created "2016-06-24" @default.
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- W2037974767 date "1987-02-01" @default.
- W2037974767 modified "2023-09-25" @default.
- W2037974767 title "Kinetic and topographical studies of the phosphatidylcholine:ceramide choline phosphotransferase in plasma membrane particles from mouse ascites cells" @default.
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- W2037974767 doi "https://doi.org/10.1016/0005-2736(87)90315-4" @default.
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