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Journal of Lipid Research, Vol. 14, 509-516, September 1973
Copyright © 1973 by Lipid Research, Inc.

Glycerolipid biosynthesis in rat adipose tissue. I. Properties and distribution of glycerophosphate acyltransferase and effect of divalent cations on neutral lipid formation

S. C. Jamdar and H. J. Fallon

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

A sensitive radioactive assay of acyl CoA:sn-glycerol-3-phosphate-O-acyltransferase (EC 2.3.1.15) was developed to study the properties and subcellular distribution of this enzyme in rat epididymal adipose tissue. The esterification of sn-glycerol-3-phosphate was measured in the presence of palmitoyl CoA or palmitate, ATP, CoA, and Mg²⁺ at pH 7.5. The presence of glycerophosphate acyltransferase was detected in both mitochondria and microsomes. The product of this reaction was identified as phosphatidate by thin-layer chromatography and dual isotope incorporation studies. Several divalent cations reduced the activity of this enzyme. Although Mg²⁺ was not required for the activity of glycerophosphate acyltransferase, its addition to the incubation mixture resulted in an increased formation of neutral lipids at the expense of phosphatidate. This result is explained by an activation of microsomal phosphatidate phosphatase (EC 3.1.3.4). The effect of Mg²⁺ was completely abolished by Ni²⁺, Co²⁺, Mn²⁺, and Zn²⁺. These studies suggest that the balance between Mg²⁺ and several other divalent ions may be important in the regulation of neutral lipid synthesis in adipose tissue.

Supplementary key words phosphatidate formation • Mg²⁺ • phosphatidate phosphatase

Submitted on September 5, 1972
Revised on March 9, 1973
Accepted on May 2, 1973

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