Huang Y P, Peter R E
Department of Zoology, University of Alberta, Edmonton, Canada.
Gen Comp Endocrinol. 1988 Feb;69(2):308-16. doi: 10.1016/0016-6480(88)90019-6.
The binding of salmon gonadotropin-releasing hormone (sGnRH) and its superactive analog, [D-Arg6, Pro9-NEt]-sGnRH, to a macromolecular component in goldfish serum was studied, using 125I-[D-Arg6, Pro9-NEt]-sGnRH and 125I-sGnRH as labeled ligands. Bound was separated from free labeled ligand by gel filtration with Sephadex G-50. The binding of labeled ligand to goldfish serum was dose-dependent. The results indicate a single class of binding site having low affinity and high capacity. The existence of a GnRH binding protein in serum may, in part, contribute to the long-lasting pharmacological action of GnRHs in goldfish.
利用125I-[D-精氨酸6，脯氨酸9-乙酯]-鲑鱼促性腺激素释放激素（sGnRH）和125I-sGnRH作为标记配体，研究了sGnRH及其超活性类似物[D-精氨酸6，脯氨酸9-乙酯]-sGnRH与金鱼血清中一种大分子成分的结合。通过用葡聚糖凝胶G-50进行凝胶过滤，将结合的部分与游离的标记配体分离。标记配体与金鱼血清的结合呈剂量依赖性。结果表明存在一类具有低亲和力和高容量的结合位点。血清中GnRH结合蛋白的存在可能部分有助于GnRHs在金鱼体内的长效药理作用。
