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The relationship between the chain elongation of palmitoyl-CoA and phospholipid content in rat liver microsomes was studied. When liver microsomes were incubated with phospholipase C, microsomal phospholipids were linearly hydrolyzed during 10 min of incubation under the present experimental conditions. Coincident with the decrease in microsomal phospholipid content by phospholipase C treatment, the chain elongation activity also decreased linearly. The decreased chain elongation activity in phospholipase C-treated microsomes was completely or partially recovered by the addition of a sonicated dispersion of phosphatidylcholine, microsomal phospholipids or phosphatidylcholine/phosphatidylethanolamine mixtures. The extent of recovery of decreased activity by a sonicated dispersion of phosphatidylcholine/phosphatidylethanolamine mixture was gradually reduced by increasing amounts of phosphatidylethanolamine in the dispersion. In addition, the chain elongation activity in native nicrosomes was more stimulated by the addition of a sonicated dispersion of phosphatidylcholine alone than by that of phosphatidylcholine/phosphatidylethanolamine mixtures. The chain elongation activity of palmitoyl-CoA was inhibited by the addition of stearoyl-CoA which is the end-product of this reaction. The inhibitory effect of stearoyl-CoA was partially eliminated by the addition of a sonicated dispersion of phosphatidylcholine. The increase of the chain elongation activity in native and phospholipase C-treated microsomes by the addition of a sonicated dispersion of phosphatidylcholine was not related to the activity of fatty acyl-CoA hydrolase.
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