Ehle H, Müller E, Horn A
FEBS Lett. 1985 Apr 22;183(2):413-6. doi: 10.1016/0014-5793(85)80822-x.
Pure alkaline phosphatase of the calf intestine is able to hydrolyze phosphatidylinositol 4,5-diphosphate (TPI) to phosphatidylinositol and Pi and to dephosphorylate phosphatidic acid. This phosphomonoesterase activity shows a considerably high specific activity when an incubation medium at neutral pH containing 3 mM deoxycholate is used. The activity is inhibited by low concentrations of Ca2+. The enzyme has no detectable phosphodiesterase activity under the conditions tested.
小牛肠碱性磷酸酶纯品能够将磷脂酰肌醇4,5-二磷酸(TPI)水解为磷脂酰肌醇和无机磷酸,并使磷脂酸脱磷酸。当使用含有3 mM脱氧胆酸盐的中性pH孵育介质时,这种磷酸单酯酶活性表现出相当高的比活性。该活性受到低浓度Ca2+的抑制。在所测试的条件下,该酶没有可检测到的磷酸二酯酶活性。