Journal of Lipid Research, Vol. 8, 456-462, September 1967
Copyright © 1967 by Lipid Research, Inc.

Phosphatidyl glycerophosphate phosphatase

Ying-Ying Chang and Eugene P. Kennedy

Department of Biological Chemistry, Harvard Medical School, Boston, Massachusetts 02115

An enzyme (phosphatidyl glycerophosphate phosphatase) that catalyzes the formation of phosphatidyl glycerol from phosphatidyl glycerophosphate has been rendered soluble by treatment of the particulate fraction of E. coli with Triton X-100 in the presence of EDTA, and has been partially purified. The enzyme is specific for phosphatidyl glycerophosphate and does not catalyze the hydrolysis of other simple phosphomonoesters. It requires Mg⁺⁺ for activity and is inhibited by sulfhydryl agents. Some other properties of the enzyme are also described.

Supplementary key words phosphatidyl glycerophosphate • phosphatidyl glycerol • enzymatic • E. coli • particulate fraction • Triton • EDTA • extraction • phosphatidic acid • alkaline phosphatase • acid phosphatase

Submitted on February 20, 1967
Accepted on April 25, 1967

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