The acylation of lysophosphatidylcholine by subcellular fractions of guinea-pig cerebral cortex.

The acylation of lysophosphatidylcholine by isolated subcellular fractions of guinea-pig cerebral cortex has been determined. The microsomal fraction contained the highest acylation activity, in terms of both specific and total activity. In all particulate fractions, including synaptic plasma membrane and mitochondria, there was a high correlation (correlation coefficient r = 0.90; P less than 0.001) between acylation and the activity of the microsomal enzyme, NADPH-cytochrome c reductase. No correlation existed between acylation and the activities of (Na+ + K+)-ATPase, acetylcholinesterase or succinate dehydrogenase. Acyl-CoA synthetase and lysophosphatidylcholine/acyltransferase, the individual enzymes responsible for acylation were enriched in the microsomal fraction. The activities of both enzymes in subcellular fractions correlated well with those of NADPH-cytochrome c reductase, with the exception that acyl-CoA synthetase activity in the mitochondrial fraction was largely independent of endoplasmic reticulum. Neither synaptic plasma membranes nor mitochondria appeared to possess significant amounts of acyltransferase activity. The results indicate that the acylation of lysophosphatidylcholine is confined to the endoplasmic reticulum, and that activity present in the synaptic plasma membrane or mitochondrial fraction is attributable to microsomal contamination.