Marshall J C, Shakespear R A, Odell W D
Clin Endocrinol (Oxf). 1976 Nov;5(6):671-7. doi: 10.1111/j.1365-2265.1976.tb03870.x.
Two specific binding sites for LHRH are present on plasma membranes prepared from rat and bovine anterior pituitary glands. One site is of high affinity (K = 2X108 1/MOL) and the second is of lower affinity (8-5X105 1/mol) and much greater capacity. Studies on membrane fractions prepared from other tissues showed the presence of a single specific site for LHRH. The kinetics and specificity of this site were similar to those of the lower affinity pituitary receptor. These results indicate that only pituitary membranes possess the higher affinity binding site and suggest that the low affinity site is not of physiological importance in the regulation of gonadotrophin secretion. After dissociation from membranes of non-pituitary tissues 125I-LHRH rebound to pituitary membrane preparations. Thus receptor binding per se does not result in degradation of LHRH and the function of these peripheral receptors remains obscure.
从大鼠和牛的垂体前叶制备的质膜上存在两种促性腺激素释放激素（LHRH）的特异性结合位点。一个位点具有高亲和力（K = 2×10⁸ 1/mol），另一个位点亲和力较低（8 - 5×10⁵ 1/mol）但容量大得多。对从其他组织制备的膜组分的研究表明存在一个单一的LHRH特异性位点。该位点的动力学和特异性与低亲和力垂体受体的相似。这些结果表明只有垂体膜具有高亲和力结合位点，并提示低亲和力位点在促性腺激素分泌调节中不具有生理重要性。从非垂体组织的膜上解离后，¹²⁵I - LHRH会重新结合到垂体膜制剂上。因此，受体结合本身不会导致LHRH降解，这些外周受体的功能仍不清楚。
