Hydrolysis of p-nitrophenylphosphorylcholine by alkaline phosphatase and phospholipase C from rabbit sperm-acrosome.
Hydrolysis of p-nitrophenylphosphorylcholine by alkaline phosphatase and phospholipase C from rabbit sperm-acrosome.
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兔精子顶体的碱性磷酸酶和磷脂酶 C 水解对硝基苯磷酰胆碱。
DOI：
10.1016/0006-291x(82)92116-7
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发表时间：
1982
影响因子：
3.1
通讯作者：
WhiteJr,RA
中科院分区：
文献类型：
--
作者：
Srivastava,PN;Brewer,JM;WhiteJr,RA
作为磷脂酶C的人工底物，对硝基苯基磷酸胆碱也容易被碱性磷酸酶水解，尽管有报道称碱性磷酸酶的活性需要末端磷酸盐。家兔精液中p-硝基苯磷酸胆碱水解活性主要集中在精子顶体或胞质液滴的Hyamine-Triton提取物中，而不是精浆中。这些提取物的圆盘电泳显示磷酸酶和磷脂酶C样活性的良好分离区。在精浆中仅观察到磷酸酶活性。提示磷脂酶C定位于精子顶体。
p-Nitrophenylphosphorylcholine, used as an artificial substrate for phospholipase C, is readily hydrolyzed by alkaline phosphatases also, despite the reported requirement of alkaline phosphatases for a terminal phosphate for activity. p-Nitrophenylphosphorylcholine hydrolyzing activity in rabbit semen is concentrated in Hyamine-Triton extracts of sperm acrosomes or cytoplasmic droplets rather than seminal plasma. Disc electrophoresis of these extracts shows well separated zones of phosphatase and phospholipase C-like activity. Only phosphatase activity is observed in seminal plasma. It is suggested that phospholipase C is located in the sperm acrosome.