Andersson E, Borg B, de Leeuw R
Department of Zoology, University of Stockholm, Sweden.
Gen Comp Endocrinol. 1989 Oct;76(1):41-5. doi: 10.1016/0016-6480(89)90030-0.
Binding sites for gonadotropin-releasing hormone (GnRH) in stickleback pituitary homogenates were characterized using an iodinated, superactive analog of salmon GnRH (sGnRH), D-Arg6-Pro9-sGnRH-NEt (sGnRHa). Binding of 125I-sGnRHa reached equilibrium after 60 min incubation at 4 degrees and was a function of tissue concentration. The specificity of 125I-sGnRHa binding was demonstrated by displacement with sGnRHa, sGnRH, and Buserelin [D-Ser(t-Bu)6-Pro9-GnRH-NEt]. Both Scatchard analyses of saturation data and displacement curves revealed a single class of high-affinity binding sites (Ka = 0.71 +/- 0.03 X 10(9) M-1, Bmax = 1087 +/- 165 fmol/mg protein).
利用碘化的鲑鱼促性腺激素释放激素（sGnRH）超活性类似物D-Arg6-Pro9-sGnRH-NEt（sGnRHa）对棘背鱼垂体匀浆中促性腺激素释放激素（GnRH）的结合位点进行了表征。125I-sGnRHa在4℃孵育60分钟后达到结合平衡，且是组织浓度的函数。通过用sGnRHa、sGnRH和布舍瑞林[D-Ser(t-Bu)6-Pro9-GnRH-NEt]进行置换，证明了125I-sGnRHa结合的特异性。对饱和数据的Scatchard分析和置换曲线均显示存在一类高亲和力结合位点（Ka = 0.71 +/- 0.03 X 10(9) M-1，Bmax = 1087 +/- 165 fmol/mg蛋白质）。
