Spanner S, Ansell G B
Neurochem Res. 1987 Feb;12(2):203-6. doi: 10.1007/BF00979538.
Experiments with glycerophosphocholine phosphodiesterase (GPC diesterase, EC 3.1.4.2.) in rat brain microsomes suggest that, although its activity is inhibited by low concentrations of calmidazolium, its dependence on Ca2+ ions is not modulated by calmodulin. The activity of glycerophosphocholine choline phosphodiesterase (choline phosphohydrolase, EC 3.1.4.38) was much lower than that of the GPC diesterase. A relatively inexpensive method for the preparation of sn-glycero-3-phospho [Me-14C]choline is described.
在大鼠脑微粒体中对甘油磷酸胆碱磷酸二酯酶（GPC二酯酶，EC 3.1.4.2.）进行的实验表明，尽管其活性受到低浓度氯氮卓的抑制，但其对钙离子的依赖性不受钙调蛋白的调节。甘油磷酸胆碱胆碱磷酸二酯酶（胆碱磷酸水解酶，EC 3.1.4.38）的活性远低于GPC二酯酶。本文描述了一种相对廉价的制备sn-甘油-3-磷酸[甲基-14C]胆碱的方法。
