Water-soluble gonadotropin receptors of the rat ovary.

Water-soluble gonadotropin receptors of the rat ovary.
复制标题

大鼠卵巢的水溶性促性腺激素受体。

DOI:
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发表时间:
1982
期刊:
影响因子:
4.8
通讯作者:
M. Dufau
M. Dufau
中科院分区:
医学2区
文献类型:
--
作者:
J. Wimalasena;M. Dufau

文献摘要

被引文献

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LH/hCG的可溶性受体的特点是在水和低离子强度的缓冲液提取物的黄体化大鼠卵巢。这些受体是对hCG和LH样促性腺激素具有高亲和力(KA = 10(10)M-1)和特异性的蛋白质。水溶性受体是稳定的,并且在冻干后保留其结合能力的60-80%。通过凝胶电泳对水溶性受体的解析证明了五种结合物质,分子量为165,000、81,000、48,000、24,000和12,000。这些发现表明,一定比例(5-10%)的卵巢LH/hCG膜受体可变为水溶性,同时保留其结合特性,LH/hCG的特异性结合位点存在于比非离子去污剂提取的主要6.5S(mol wt,194,000)形式小得多的蛋白质中。这些小LH结合位点的稳定性对于进一步纯化和分析促性腺激素结合的结构决定簇是有价值的。
Soluble receptors for LH/hCG were characterized in aqueous and low ionic strength buffer extracts of the luteinized rat ovary. These receptors are proteins with high affinity (KA = 10(10) M-1) and specificity for hCG- and LH-like gonadotropins. The water-soluble receptors are stable and retained 60-80% of their binding capacity after lyophilization. Resolution of the water-soluble receptors by gel electrophoresis demonstrated five binding species, with molecular weights of 165,000, 81,000, 48,000, 24,000 and 12,000. These findings have demonstrated that a proportion (5-10%) of ovarian LH/hCG membrane receptors can be rendered water soluble with preservation of their binding properties and that the specific binding site for LH/hCG is present in proteins much smaller than the predominant 6.5S (mol wt, 194,000) form extracted by nonionic detergents. The stability of these small LH-binding sites is of value for further purification and analysis of structural determinants for gonadotropin binding.