Cibert C
Biol Cell. 1985;55(1-2):63-9. doi: 10.1111/j.1768-322x.1985.tb00410.x.
The high salt extract obtained from demembranated human spermatozoa contains high molecular weight proteins. These proteins are associated with an ATPase activity inhibited by sodium orthovanadate. In association with lower molecular weight proteins, they constitute a 20 S particle and are probably localized in the dynein arms (and in the radial spokes) of the human spermatozoon axonemes. Evidence is shown for a biochemical analogy between the dynein ATPases extracted from the invertebrate axonemes and the human dynein-like ATPase described in this study.
从脱膜的人类精子中获得的高盐提取物含有高分子量蛋白质。这些蛋白质与被正钒酸钠抑制的ATP酶活性相关。与低分子量蛋白质一起,它们构成一个20 S颗粒,可能定位于人类精子轴丝的动力蛋白臂(和放射辐条)中。有证据表明,从无脊椎动物轴丝中提取的动力蛋白ATP酶与本研究中描述的人类动力蛋白样ATP酶之间存在生化相似性。