Incorporation of [1-14C]Palmitoyl-CoA into Phosphatidylcholine by Plasma Membranes of Rat Submaxillary Glands in vitro

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Abstract
On incubation with the isolated rat submaxillary gland plasma membranes, [1-14C]palmitoyl-CoA was incorporated mainly into phosphatidylcholine and hydrolyzed to [1-14C]palmitic acid and CoASH. The addition of lysophosphatidylcholine enhanced the incorporation into phosphatidylcholine and lowered the hydrolysis of palmitoyl-CoA markedly. In the presence of lysophosphatidylcholine, palmitoyl-CoA incorporation into phosphatidylcholine was maximum at 0.1 mM palmitoyl-CoA, 0.5 mM lysophosphatidylcholine and between pH 7.0-9.0. The incorporation into phosphatidylcholine was stimulated by Na+, K+ and F-, inhibited by Ca2+ and Mg2+ and unaffected by sodium deoxycholate and ATP. Epinephrine inhibited the incorporation of palmitoyl-CoA into phosphatidylcholine in the presence or absence of ATP, the inhibition being more in the presence of ATP than in its absence. Dibutyryl AMP mimicked the inhibitory effect of epinephrine.

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