Rao V N, Bhargava P M
Biochem J. 1985 Apr 15;227(2):609-19. doi: 10.1042/bj2270609.
The isolation from bovine seminal plasma and purification of a new protein called 'antiseminalplasmin', which reverses the inhibition of the growth of, and RNA synthesis in, Escherichia coli by seminalplasmin (another protein of bovine seminal plasma), is described. Antiseminalplasmin, a weakly acidic protein, has a minimum Mr of about 39 000 and appears to consist of three acidic peptide chains that move close to each other on electrophoresis on cellulose acetate strips or on sodium dodecyl sulphate/18%-(w/v)-polyacrylamide gels. Antiseminalplasmin has a tendency to oligomerize at slightly alkaline pH values; it does not bind to seminalplasmin or to DNA, and does not reverse the inhibition by seminalplasmin of transcription in vitro by purified E. coli RNA polymerase. It appears that antiseminalplasmin may act by binding to the cell surface and preventing the entry of seminalplasmin into the cells. By itself, antiseminalplasmin has no effect on the growth of E. coli.
本文描述了从牛精浆中分离并纯化一种名为“抗精浆溶素”的新蛋白质的过程。精浆溶素（牛精浆中的另一种蛋白质）会抑制大肠杆菌的生长及RNA合成，而抗精浆溶素能逆转这种抑制作用。抗精浆溶素是一种弱酸性蛋白质，最小相对分子质量约为39000，似乎由三条酸性肽链组成，在醋酸纤维素条或十二烷基硫酸钠/18%（w/v）聚丙烯酰胺凝胶上电泳时，它们彼此靠近迁移。抗精浆溶素在略碱性pH值下有形成寡聚物的倾向；它不与精浆溶素或DNA结合，也不能逆转精浆溶素对纯化的大肠杆菌RNA聚合酶体外转录的抑制作用。抗精浆溶素似乎可能通过与细胞表面结合，阻止精浆溶素进入细胞来发挥作用。抗精浆溶素本身对大肠杆菌的生长没有影响。
