J. Lipid Res.
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Journal of Lipid Research, Vol. 9, 652-660, September 1968
Copyright © 1968 by Lipid Research, Inc.

Acylation of sn-glycerol 3-phosphate by cell fractions of rat liver

Harold J. Fallon and Robert G. Lamb

Departments of Medicine and Biochemistry, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27514

The esterification of sn-glycerol 3-(dihydrogen phosphate) with long-chain fatty acids by rat liver microsomal preparations has been studied. A newly modified spectrophotometric assay for glycerolphosphate acyltransferase (GP-acyltransferase) compared favorably with other assay methods, including measurement of the incorporation of sn-glycerol-14C 3-(dihydrogen phosphate) into glycerolipids. Cofactor requirements, preliminary kinetic constants, and optimum pH were determined. The product of the reaction was identified as monoacylglycerophosphate by thin-layer chromatography.

Albumin activated GP-acyltransferase at low concentrations of acyl CoA but was inhibitory at higher concentrations. Serum ßbeta;-lipoprotein also caused activation of GP-acyltransferase. The effect of albumin could not be attributed to binding of substrate or fatty acids or the provision of metal ions.

Diacylglycerophosphate, cytidine triphosphate, sulfhydryl binding agents, and sodium palmitate were identified as inhibitors of microsomal GP-acyltransferase. The physiological significance of these inhibitors remains to be established.

Supplementary key words sn-glycerol 3-phosphate • acyltransferase • modified spectrophotometric assay • activation • inhibition • albumin • serum proteins • metal ions

Submitted on February 26, 1968
Accepted on June 6, 1968


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