Elgavish A, Pillion D J, Meezan E
Department of Pharmacology, University of Alabama, Birmingham 35294.
Life Sci. 1989;44(15):1037-42. doi: 10.1016/0024-3205(89)90555-9.
[125I]VIP (vasoactive intestinal peptide) bound to apical membranes isolated from the bovine tracheal epithelium with a half maximal inhibition by unlabeled VIP (IC50) of 0.6 x 10(-9)M and binding was reversible. Glucagon did not affect [125I]VIP binding to the membranes. [125I]VIP was covalently cross-linked to tracheal membrane proteins using disuccinimidyl suberate. SDS-polyacrylamide gel electrophoresis of labeled tracheal membranes revealed one major [125I]-receptor complex of Mr = 71,000 to which binding of [125I]VIP was inhibited by 10 microM unlabeled VIP. These results are consistent with the presence of a specific, high-affinity receptor for VIP, with a Mr = 71,000, in apical membrane vesicles isolated from the bovine tracheal epithelium.
[125I]血管活性肠肽（VIP）与从牛气管上皮分离的顶端膜结合，未标记的VIP产生半数最大抑制浓度（IC50）为0.6×10⁻⁹M，且结合是可逆的。胰高血糖素不影响[125I]VIP与该膜的结合。使用辛二酸二琥珀酰亚胺酯将[125I]VIP与气管膜蛋白共价交联。标记的气管膜的十二烷基硫酸钠-聚丙烯酰胺凝胶电泳显示一个主要的Mr = 71,000的[125I]受体复合物，10微摩尔未标记的VIP可抑制[125I]VIP与该复合物的结合。这些结果与在从牛气管上皮分离的顶端膜囊泡中存在一种特异性、高亲和力的Mr = 71,000的VIP受体一致。
