Hume M E, Siegel M S, Polakoski K L
J Androl. 1987 Jul-Aug;8(4):221-4. doi: 10.1002/j.1939-4640.1987.tb03309.x.
A comparison of the alkaline proteinase activity of human seminal plasma, the seminal non-gamete cellular material and spermatozoa was made by gelatin-sodium dodecyl sulfate-polyacrylamide gel electrophoresis (gelatin-SDS-PAGE) zymography. Several major (molecular weights = greater than 56,000) and minor (35,000 to 44,000) bands of proteinase activity were seen in the seminal plasma samples from nonvasectomized and vasectomized, healthy donors. Similar activity profiles were observed in the nongamete cellular material of vasectomized donor ejaculates. The major proteinase activity in sperm extracts was in the 47,000 to 55,000 (proacrosin-acrosin) and 34,000 to 37,000 (sperminogen-spermin) molecular weight ranges. These results suggest that the proacrosin-acrosin and sperminogen-spermin systems are of sperm origin and that there are considerable amounts of larger molecular weight trypsin-like enzymes in the soluble and nongamete cellular material of human seminal plasma.
采用明胶-十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（明胶-SDS-PAGE）酶谱法对人类精浆、精液非配子细胞物质和精子的碱性蛋白酶活性进行了比较。在未行输精管切除术和已行输精管切除术的健康供体的精浆样本中，可见几条主要的（分子量＞56,000）和次要的（35,000至44,000）蛋白酶活性条带。在已行输精管切除术的供体射精的非配子细胞物质中观察到类似的活性谱。精子提取物中的主要蛋白酶活性在分子量47,000至55,000（前顶体蛋白酶-顶体蛋白酶）和34,000至37,000（精子原-精子素）范围内。这些结果表明，前顶体蛋白酶-顶体蛋白酶和精子原-精子素系统起源于精子，并且在人类精浆的可溶性和非配子细胞物质中存在大量分子量较大的类胰蛋白酶。
