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Journal of Lipid Research, Vol. 8, 447-455, September 1967
Copyright © 1967 by Lipid Research, Inc.
Department of Biological Chemistry, Harvard Medical School, Boston, Massachusetts 02115
An enzyme (l-glycerol 3-phosphate: CMP phosphatidyltransferase) catalyzing the synthesis of phosphatidyl glycerophosphate from CDP-diglyceride and l-glycerol 3-phosphate has been rendered soluble by treatment of the particulate, membrane-containing fraction of E. coli with Triton X-100 and has been partially purified. The enzyme, devoid of phosphatidyl glycerophosphatase activity, is specific for l-glycerol 3-phosphate and is completely dependent upon added Mg++ or Mn++ for activity. It has high affinity for CDP-diglyceride and can be used for the assay of this nucleotide.
Other properties of the enzyme are also described.
Supplementary key words phosphatidyl • glycerophosphate • CDP-diglyceride • l-glycerol 3-phosphate • enzymatic • biosynthesis • E. coli • particulate fraction • Triton • extraction
Submitted on February 20, 1967
Accepted on April 25, 1967
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