Pagelson G, Zohar Y
National Center for Mariculture, Israel Oceanographic and Limnological Research Institute, Eilat.
Biol Reprod. 1992 Dec;47(6):1004-8. doi: 10.1095/biolreprod47.6.1004.
Receptors for GnRH in the pituitary of Sparus aurata were characterized using iodinated [D-Ala6-Pro9-NEt]-LHRH (GnRHa). Equilibrium binding of the ligand to the receptor was achieved after 1 h at 4 degrees C. Binding of the radioligand was a function of tissue concentration, with a linear correlation over the range of one-sixteenth to three-fourths pituitary per tube. Displacement experiments with salmon GnRH (sGnRH), GnRHa, as well as unrelated peptides demonstrated the specificity of the receptors. Binding was found to be saturable at ligand concentrations of 4 x 10(-9) M. Scatchard analysis of the saturation data suggested the presence of a single class of high-affinity sites (Ka = 0.567 +/- 0.136 x 10(9) M-1, Bmax = 1091 +/- 207 fmol/mg protein).
利用碘化的[D - Ala6 - Pro9 - NEt] - LHRH（促性腺激素释放激素类似物，GnRHa）对金头鲷垂体中的促性腺激素释放激素（GnRH）受体进行了表征。在4℃下1小时后，配体与受体达到平衡结合。放射性配体的结合是组织浓度的函数，在每管十六分之一至四分之三垂体的范围内呈线性相关。用鲑鱼促性腺激素释放激素（sGnRH）、促性腺激素释放激素类似物以及无关肽进行的置换实验证明了受体的特异性。发现在配体浓度为4×10⁻⁹ M时结合是可饱和的。对饱和数据的Scatchard分析表明存在一类单一的高亲和力位点（Ka = 0.567 ± 0.136×10⁹ M⁻¹，Bmax = 1091 ± 207 fmol/mg蛋白质）。
