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Journal of Lipid Research, Vol. 14, 517-524, September 1973
Copyright © 1973 by Lipid Research, Inc.

Glycerolipid synthesis in rat adipose tissue. II. Properties and distribution of phosphatidate phosphatase

S. C. Jamdar and H. J. Fallon

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

The properties and subcellular distribution of phosphatidate phosphatase (EC 3.1.3.4) from adipose tissue have been investigated. The enzyme was assayed using both aqueous phosphatidate and membrane-bound phosphatidate as substrates. When measured with aqueous substrate, activity was detected in the mitochondria, the microsomes, and the soluble fraction. Mg²⁺ at low concentration stimulated the phosphatidate phosphatase from soluble and microsomal fractions but had no effect on the mitochondrial phosphatidate phosphatase. At higher concentration Mg²⁺ was inhibitory. In the presence of Mg²⁺, the phosphatidate phosphatase from soluble and microsomal fractions was active against membrane-bound phosphatidate. No activity was demonstrated with membrane-bound substrate in the absence of Mg²⁺. Mitochondria did not contain activity toward the membrane-bound substrate. The rate of utilization of aqueous phosphatidate was always higher than that of membrane-bound substrate. These results indicate that there are at least two different phosphatidate phosphatases in adipose tissue.

Supplementary key words aqueous phosphatidate • membrane-bound phosphatidate • Mg²⁺

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

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