Chang Y Y, Kennedy E P
J Lipid Res. 1967 Sep;8(5):456-62.
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.
一种催化磷脂酰甘油磷酸形成磷脂酰甘油的酶（磷脂酰甘油磷酸磷酸酶），通过在EDTA存在的情况下用 Triton X-100处理大肠杆菌的颗粒部分而变得可溶，并已被部分纯化。该酶对磷脂酰甘油磷酸具有特异性，不催化其他简单磷酸单酯的水解。它的活性需要Mg(++)，并受到巯基试剂的抑制。还描述了该酶的一些其他特性。
