Renoir J M, Mercier-Bodard C, Baulieu E E
Proc Natl Acad Sci U S A. 1980 Aug;77(8):4578-82. doi: 10.1073/pnas.77.8.4578.
Sex steoid binding plasma protein (Sbp) in man and in monkeys binds the androgens dihydrotestosterone and testosterone and the estrogen estradiol with high affinity (Kd approximately 0.5, 1, and 2 nM, respectively). Detailed studies of steroid binding specificity give the same results in all primates, except that in humans and chimpanzees estrone does not compete for dihydrotestosterone binding. In other mammals, Sbps of Artiodactyla and Lagomorpha have the same range of affinities for androgens but they do not bind estradiol to any significant extent (Kd > 280 nM). The dog has an unusual Sbp (Kd for dihydrotestosterone, 7.1 nM; for estradiol, 125 nM), and rodents do not have a specific dihydrotestosterone-binding plasma protein. Gel filtration and immunoelectrophoretic experiments have been performed with a monospecific antiserum against human Sbp. The results indicate variable crossreactivities with Sbps of primates (from complete in chimpanzee and gorilla to weak in Prosimii). No crossreaction was observed with specific androgen-binding plasma proteins of other species. These results suggest the evolutionary emergence of bifunctional Sbp.
人类和猴子体内的性类固醇结合血浆蛋白(Sbp)能以高亲和力(解离常数Kd分别约为0.5、1和2纳摩尔)结合雄激素双氢睾酮和睾酮以及雌激素雌二醇。除了人类和黑猩猩中雌酮不竞争双氢睾酮结合位点外,对类固醇结合特异性的详细研究在所有灵长类动物中都得到了相同的结果。在其他哺乳动物中,偶蹄目动物和兔形目动物的Sbps对雄激素具有相同范围的亲和力,但它们在很大程度上不结合雌二醇(Kd>280纳摩尔)。狗有一种不同寻常的Sbp(双氢睾酮的Kd为7.1纳摩尔;雌二醇的Kd为125纳摩尔),而啮齿动物没有特异性的双氢睾酮结合血浆蛋白。已经用针对人类Sbp的单特异性抗血清进行了凝胶过滤和免疫电泳实验。结果表明与灵长类动物的Sbps有不同程度的交叉反应(从黑猩猩和大猩猩中的完全交叉反应到原猴亚目的弱交叉反应)。未观察到与其他物种的特异性雄激素结合血浆蛋白有交叉反应。这些结果提示了双功能Sbp的进化出现。