Singer A G, Clancy A N, Macrides F, Agosta W C, Bronson F H
Rockefeller University, New York, New York 10021.
Biol Reprod. 1988 Feb;38(1):193-9. doi: 10.1095/biolreprod38.1.193.
Female mouse urine contains a pheromone that acts via the vomeronasal organ of conspecific males to stimulate a rapid increase in circulating levels of luteinizing hormone. A bioassay based on this male response was used to test biochemical preparations of female urine. Retention of significant biological activity by the urine after dialysis indicated that the activity is associated with urinary protein. Complete loss of activity from the urine after adsorption chromatography on a neutral polystyrene column suggested that the protein functions as a pheromone carrier. Assay of gel permeation chromatography fractions, before and after degradation of the urinary proteins with proteolytic enzymes, demonstrated that the protein is not necessary for the male response in the bioassay. Its resistance to vigorous proteolytic enzyme treatment further indicates that the pheromone is not a peptide. High biological activity, indistinguishable from that of the unfractionated urine, was isolated in a protein-depleted, presumably low molecular weight fraction containing compounds that are retarded by adsorption on Sephadex. The chemical properties of this female mouse pheromone are markedly different from those of a recently purified female hamster pheromone that also acts via the vomeronasal organ.
雌性小鼠尿液中含有一种信息素，它通过同种雄性小鼠的犁鼻器起作用，刺激促黄体生成素的循环水平迅速升高。基于这种雄性反应的生物测定法被用于检测雌性尿液的生化制剂。透析后尿液仍保留显著的生物活性，这表明该活性与尿蛋白有关。在中性聚苯乙烯柱上进行吸附色谱后，尿液的活性完全丧失，这表明该蛋白起到了信息素载体的作用。在用蛋白水解酶降解尿蛋白之前和之后，对凝胶渗透色谱馏分进行测定，结果表明该蛋白在生物测定中对雄性反应并非必需。它对剧烈的蛋白水解酶处理具有抗性，这进一步表明该信息素不是一种肽。在一个蛋白质耗尽、可能是低分子量的馏分中分离出了与未分级尿液的生物活性无法区分的高生物活性物质，该馏分中含有因吸附在葡聚糖凝胶上而滞留的化合物。这种雌性小鼠信息素的化学性质与最近纯化的同样通过犁鼻器起作用的雌性仓鼠信息素的化学性质明显不同。
