Veliçelebi G, Santacroce T M, Harpold M M
Biochem Biophys Res Commun. 1985 Jan 16;126(1):33-9. doi: 10.1016/0006-291x(85)90567-4.
We have studied the specific binding of a synthetic 40 amino acid, free carboxy terminus analog of human pancreatic growth hormone releasing factor (hp GRF-40-OH) to partially purified homogenates of bovine anterior pituitaries. The binding of hpGRF-40-OH to pituitary receptors at 4 degrees C reached maximal level in 4 hours and remained steady for the next 18 hours. Specific binding increased linearly with the amount of protein present in the assay. 125I-hpGRF-40-OH binding to pituitary homogenates was competitively inhibited by hpGRF-40-OH but not by unrelated hormones. The competition curve and Scatchard analysis suggest the presence of single class of receptors with a Kd congruent to 3nM and binding capacity of approximately 200 fmoles/mg protein. This is the first demonstration of specific receptors for GRF on anterior pituitary cells.
我们研究了一种合成的含40个氨基酸、具有游离羧基末端的人胰腺生长激素释放因子类似物（hp GRF - 40 - OH）与牛垂体前叶部分纯化匀浆的特异性结合。在4℃下，hpGRF - 40 - OH与垂体受体的结合在4小时内达到最大水平，并在接下来的18小时内保持稳定。特异性结合随测定中蛋白质含量呈线性增加。125I - hpGRF - 40 - OH与垂体匀浆的结合受到hpGRF - 40 - OH的竞争性抑制，但不受无关激素的抑制。竞争曲线和Scatchard分析表明存在一类单一的受体，其解离常数（Kd）约为3nM，结合能力约为200飞摩尔/毫克蛋白质。这是首次在前垂体细胞上证明生长激素释放因子（GRF）的特异性受体。
