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- W2103446449 abstract "Cholinephosphotransferase in microsomes from developing safflower cotyledons incorporated radioactivity from [14C]CDPcholine into phosphatidylcholine at rates of 6–10 nmol/mg protein per min. The enzyme required Mg2+ for activity, had a pH optimum of 8 and was inhibited by Ca2+ and CMP. Diacylglycerols from a mixture of molecular species were incorporated into the phospholipid in proportion to the amount of each available. Labelled diacylglycerols and CDPcholine were produced at about 1 nmol/mg protein per min by the cholinephosphotransferase-catalysed back-reaction from phosphatidylcholine, labelled in the diacylglycerol and choline moieties, respectively. Prolonged incubation of microsomes with [14C]CDPcholine resulted in the specific radioactivities of CDPcholine and phosphatidylcholine reaching similar values. When microsomes containing diacylglycerols and phosphatidylcholine with differing acyl compositions were incubated with CMP plus CDPcholine, the acyl composition of the smaller diacylglycerol pool changed markedly towards that of the phosphatidylcholine. These results suggest that the reversible reaction catalysed by cholinephosphotransferase causes the equilibration of the phosphorylcholine and diacylglycerol moieties of phosphatidylcholine with those of CDPcholine and the microsomal diacylglycerol pool, respectively. During cotyledon development, the period of maximum cholinephosphotransferase activity coincided with the fastest rates of phosphatidylcholine and triacylglycerol accumulation. At this time the enzyme's activity in vitro was 100-fold greater than the in vivo rate of accumulation of the phospholipid." @default.
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- W2103446449 date "1985-03-01" @default.
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- W2103446449 title "Some properties of cholinephosphotransferase from developing safflower cotyledons" @default.
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- W2103446449 doi "https://doi.org/10.1016/0005-2760(85)90101-8" @default.
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