Ransom R W, Young G S, Schneck K, Goodman C B
Department of New Lead Pharmacology, Merck Sharp & Dohme Research Laboratories, West Point, PA 19486-0004.
Biochem Pharmacol. 1992 Apr 15;43(8):1823-7. doi: 10.1016/0006-2952(92)90716-v.
Bradykinin (BK) B2 receptors in guinea pig ileum were characterized in both membrane and soluble form. [3H]BK bound to a single class of sites with almost identical affinities in membranes prepared from the longitudinal muscle, circular muscle and mucosal layers of the ileum. The pharmacology of the binding in the distinct layers was indistinguishable. The detergent 3-[(3-cholamidopropyl)-dimethylammonio]-1-propane sulfonate (CHAPS) maximally solubilized nearly 80% of membrane binding activity in a very stable conformation. In soluble preparations, [3H]BK labeled a single class of sites but with about 10-fold lower affinity. The affinities of BK analogs in competition studies were similarly reduced. There was no difference in the pharmacology of the binding in soluble receptors prepared from the different layers of the ileum. The results show that the ileum is a good source of solubilized B2 receptors and that the receptors in the smooth muscle and the mucosa are very similar.
对豚鼠回肠中的缓激肽（BK）B2受体进行了膜形式和可溶性形式的特性研究。[3H]BK在从回肠纵肌、环肌和黏膜层制备的膜中与单一类别的位点结合，亲和力几乎相同。不同层中结合的药理学特性无法区分。去污剂3-[(3-胆酰胺丙基)-二甲基铵]-1-丙烷磺酸盐（CHAPS）以非常稳定的构象最大程度地溶解了近80%的膜结合活性。在可溶性制剂中，[3H]BK标记单一类别的位点，但亲和力约低10倍。BK类似物在竞争研究中的亲和力也同样降低。从回肠不同层制备的可溶性受体中结合的药理学特性没有差异。结果表明，回肠是可溶性B2受体的良好来源，并且平滑肌和黏膜中的受体非常相似。
