Hierowski M T, Altamirano P, Redding T W, Schally A V
FEBS Lett. 1983 Apr 5;154(1):92-6. doi: 10.1016/0014-5793(83)80881-3.
Quantitative analyses of LH-RH-like membrane receptors were performed in five tumors from the transplantable Dunning R3372H rat prostatic adenocarcinoma. The binding of D-Trp6-LH-RH, an agonist of LH-RH, was observed in all 5 tumors. The antagonist [Ac-Dp-Cl-Phe1,2,D-Trp3,D-Lys6, D-Ala10]-LH-RH was bound to 4 tumors. The apparent equilibrium dissociation constant (Kd) for D-Trp6-LH-RH receptor was from 2.6-3.9 x 10(-10) M. The apparent equilibrium Bmax values (maximum number of binding sites) were from 17.2-86.0 fmol/mg membrane protein for D-Trp6-LH-RH receptor. The Kd for the antagonist was from 2.4-2.7 x 10(-10) M and the Bmax values were from 35.5-66.0 fmol/mg membrane protein. Similar binding studies performed in 6 normal rat prostates showed no binding capacities.
对可移植的邓宁R3372H大鼠前列腺腺癌的5个肿瘤进行了促黄体生成激素释放激素(LH-RH)样膜受体的定量分析。在所有5个肿瘤中均观察到LH-RH激动剂D-色氨酸6-LH-RH的结合。拮抗剂[乙酰基-D-对氯苯丙氨酸1,2,D-色氨酸3,D-赖氨酸6,D-丙氨酸10]-LH-RH与4个肿瘤结合。D-色氨酸6-LH-RH受体的表观平衡解离常数(Kd)为2.6 - 3.9×10⁻¹⁰ M。D-色氨酸6-LH-RH受体的表观平衡最大结合量(Bmax值,即结合位点的最大数量)为17.2 - 86.0 fmol/mg膜蛋白。拮抗剂的Kd为2.4 - 2.7×10⁻¹⁰ M,Bmax值为35. A5 - 66.0 fmol/mg膜蛋白。在6个正常大鼠前列腺中进行的类似结合研究未显示出结合能力。