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Journal of Lipid Research, Vol. 14, 466-474, July 1973
Copyright © 1973 by Lipid Research, Inc.

Diglyceride kinase in human platelets

Frank L. Call II and Mary Rubert

Department of Medicine, State University of New York, Syracuse, New York 13210

Human platelets contain diglyceride kinase, an enzyme that catalyzes the phosphorylation of diacylglycerol by adenosine 5'-triphosphate to yield phosphatidic acid. The majority of the platelet enzyme is particulate-bound, and membrane fractions of platelet homogenates have a higher specific activity than granule fractions. Both deoxycholate and magnesium are necessary for optimal enzyme activity. The K_m of the enzyme for adenosine 5'-triphosphate is 1.3 mm, and the apparent K_m for diacylglycerol is 0.4 mm. The pH optimum is 6.6-6.8 in imidazole-HCl or maleate-NaOH buffer. The enzyme activity of platelets from normal subjects was similar to the activity from patients with renal and hepatic failure.

Supplementary key words 1,2-diacylglycerol • diolein • monoolein • adenosine 5'-triphosphate • phosphatidic acid • deoxycholate • erythrocyte membranes • lymphocytes

Submitted on August 21, 1972
Revised on March 8, 1973
Accepted on March 28, 1973

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