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Formation of diacyl‐ and alkylacylphosphatidylcholine by the membranes of human platelets
Author(s) -
McKean Margaret L.,
Silver Melvin J.,
Authi Kalwant S.,
Crawford Neville
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80125-9
Subject(s) - membrane , arachidonic acid , intracellular , chemistry , transferase , biochemistry , acceptor , linoleic acid , platelet , fatty acid , chromatography , enzyme , biology , physics , immunology , condensed matter physics
We have investigated the distribution and fatty acid preference of two acyl‐CoA transferase activities in a human platelet mixed membrane fraction and in well‐characterised surface and intracellular membrane subfractions prepared from it by high‐voltage free‐flow electrophoresis. One transferase inserts long‐chain unsaturated fatty acids into 1‐acyllysophosphatidylcholine (1‐acyl‐LPC) and the other into lyso‐platelet‐activating factor (LPAF). Both transferase activities were approx. 4‐fold enriched in the intracellular membranes with respect to their specific activities in the mixed membranes. The surface membrane activities were correspondingly depleted. Using 1‐acyl‐LPC as the acceptor, all the intracellular membrane preparations showed transferase preference for the CoA ester of 8, 11, 14‐eicosatrienoic acid. In contrast when LPAF was the acceptor the CoA esters of linoleic and arachidonic acid were the preferred donors.