Arilla E, Roca B, Prieto J C
Peptides. 1986 Sep-Oct;7(5):741-4. doi: 10.1016/0196-9781(86)90088-4.
Specific binding sites for somatostatin have been characterized in cytosolic fraction of rabbit renal papilla. The interaction of 125I-Tyr11-somatostatin with cytosolic fraction was rapid, reversible, specific, saturable and dependent on temperature. At 25 degrees C the binding data were compatible with the existence of two classes of binding sites: a high-affinity class with a Kd = 57.7 nM and a low-affinity class with a Kd = 217.4 nM. Somatostatin binding sites exhibited a high degree of specificity since neuropeptides such as Leu-enkephalin, neurotensin, substance P, vasopressin and vasoactive intestinal peptide behaved as ligands with null or very low affinity.
已在兔肾乳头的胞质部分鉴定出生长抑素的特异性结合位点。125I-酪氨酸11-生长抑素与胞质部分的相互作用迅速、可逆、特异、可饱和且依赖于温度。在25℃时，结合数据与两类结合位点的存在相符：一类高亲和力位点，其解离常数（Kd）=57.7 nM；另一类低亲和力位点，其Kd = 217.4 nM。生长抑素结合位点表现出高度特异性，因为诸如亮氨酸脑啡肽、神经降压素、P物质、血管加压素和血管活性肠肽等神经肽作为配体时亲和力为零或非常低。
