Arilla E, Colás B, Prieto J C
Biosci Rep. 1986 Mar;6(3):283-91. doi: 10.1007/BF01115157.
The binding of somatostatin was studied in the cytosolic fraction of bovine gallbladder mucosa. The binding reaction depended on time, temperature and pH, and was reversible, saturable and specific. Stoichiometric data suggested the presence of two classes of binding sites: a class with high affinity (Kd = 23.6 nM) and low capacity (3.7 pmol somatostatin/mg protein) and a class with low affinity (Kd = 284.6 nm) and high capacity (85.0 pmol somatostatin/mg protein) at 37 degrees C and pH 7.4. The binding sites were highly specific for somatostatin since peptides such as [Leu]enkephalin, neurotensin, vasoactive intestinal peptide and substance P showed practically no effect upon somatostatin binding. The presence of somatostatin-binding sites in the cytosolic fraction of gallbladder mucosa, together with the known occurrence of somatostatin nerve endings in the gallbladder strongly suggests that this peptide may be involved in the physiology and physiopathology of gallbladder mucosa.
对牛胆囊黏膜胞质部分中生长抑素的结合情况进行了研究。结合反应取决于时间、温度和pH值，并且是可逆的、可饱和的和特异的。化学计量学数据表明存在两类结合位点：一类在37℃和pH 7.4条件下具有高亲和力（解离常数Kd = 23.6 nM）和低容量（3.7 pmol生长抑素/毫克蛋白质），另一类具有低亲和力（Kd = 284.6 nM）和高容量（85.0 pmol生长抑素/毫克蛋白质）。这些结合位点对生长抑素具有高度特异性，因为诸如亮氨酸脑啡肽、神经降压素、血管活性肠肽和P物质等肽对生长抑素的结合几乎没有影响。胆囊黏膜胞质部分中存在生长抑素结合位点，再加上已知胆囊中存在生长抑素神经末梢，这强烈表明该肽可能参与胆囊黏膜的生理和病理生理过程。
