Purification and characterization of a sperm motility inhibitor in human seminal plasma.
Purification and characterization of a sperm motility inhibitor in human seminal plasma.
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人精浆中精子活力抑制剂的纯化和表征。
DOI：
10.1002/j.1939-4640.1988.tb01069.x
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发表时间：
1988
影响因子：
--
通讯作者：
Claude Gagnon
中科院分区：
文献类型：
--
作者：
Teruaki Iwamoto;Claude Gagnon
从人精浆中分离纯化了一种精子运动抑制剂。纯化过程包括透析、SP-Sephadex C-25离子交换层析和羟基磷灰石吸附层析。用这种方法，精浆运动抑制剂纯化290倍，抑制活性回收率为24%。通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳估计其分子量为18，000至22，000，但根据天然条件下的分子筛，其分子量为13，000至15，000。该迁移率抑制剂的等电点为pH 9.1。它在宽的pH值范围内（5至10）和高达60 ℃的温度下是稳定的。精浆因子以浓度依赖性方式抑制纯化牛动力蛋白ATP酶的观察结果可能表明，它通过干扰动力蛋白臂功能来阻断脱膜精子的运动。
A sperm motility inhibitor from human seminal plasma was purified and characterized. The purification procedure includes dialysis, ion exchange chromatography on SP-Sephadex C-25 and adsorption chromatography on hydroxylapatite. With this procedure, the seminal plasma motility inhibitor was purified 290-fold with a 24% recovery in inhibitory activity. Its molecular weight has been estimated at 18,000 to 22,000 by sodium dodecyl sulfate polyacrylamide gel electrophoresis, but at 13,000 to 15,000 according to molecular sieving under native conditions. The mobility inhibitor has an isoelectric point pH 9.1. It is stable over a wide range of pH (5 to 10) and at temperatures up to 60 C. The observation that the seminal plasma factor inhibited purified bull dynein ATPase in a concentration-dependent manner may suggest that it blocks the motility of demembranated spermatozoa by interfering with dynein arm function.