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- W2019997129 abstract "Phospholipid acyltransferase activities of plasma membranes have been investigated with various acyl-CoA thioesters (palmitoyl, stearoyl, oleoyl, linoleoyl and arachidonoyl) with and without added lysoderivatives. Different patterns of incorporation were observed for each acyl-CoA into endogenous phosphatidylcholine and phosphatidylethanolamine. The turnover rates calculated with tracer amounts of 10 μM acyl-CoA thioesters were five times faster for the polyunsaturated than for the saturated acyl moieties of phosphatidylethanolamine and phosphatidylcholine. Arachidonoyl-CoA was the best acyl donor at low concentrations and the maximal turnover rate was observed at about 25 μM. No saturation appeared at up to 100 μM linoleoyl-CoA. Linoleoyl-CoA transacylase acylated the lyso-compounds in the following order: lysophosphatidylcholine ⪢ lysophosphatidylserine and lysophosphatidylinositol, while lysophosphatidylethanolamine inhibited linoleate incorporation into the phosphatidylethanolamine itself. Linoleoyl-CoA transacylation was not affected by the fatty acyl moiety at the 1-position of the lysophosphatidylcholine. The results support the view that the plasma membrane acyltransferase activity might contribute to the formation of bile phosphatidylcholines." @default.
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- W2019997129 date "1980-04-01" @default.
- W2019997129 modified "2023-09-29" @default.
- W2019997129 title "Acylation of endogenous phospholipids and added lysoderivatives by rat liver plasma membranes" @default.
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- W2019997129 doi "https://doi.org/10.1016/0005-2760(80)90056-9" @default.
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