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- W994441982 abstract "This chapter describes the assay method, purification procedure, and properties of phosphorylcholine-ceramide transferase. The enzyme is assayed by measuring the conversion of cytidine diphosphate choline (CDP-choline) labeled with choline-l,2-C14 to an alkali-stable phospholipid in the presence of a ceramide (fatty acid amide of sphingosine). The sphingosine moiety of the ceramide must possess the threo-trans structure for maximum activity. The enzyme is highly specific for CDP-choline. It is active with ceramides containing isomers of sphingosine with the threo configuration of the substituents at carbons 2 and 3, and with a trans double bond (or triple bond) at carbon 4, and much less active if the sphingosine moiety has the erythro configuration or a cis double bond. The enzyme requires manganese ions for optimum activity; magnesium also activates, but to a lesser extent. Calcium and barium ions inhibit the reaction. The pH optimum for phosphorylcholine-ceramide transferase is about 7.8." @default.
- W994441982 created "2016-06-24" @default.
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- W994441982 date "1962-01-01" @default.
- W994441982 modified "2023-09-25" @default.
- W994441982 title "[65e] Phosphorylcholine-ceramide transferase" @default.
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- W994441982 doi "https://doi.org/10.1016/s0076-6879(62)05265-9" @default.
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