Shreeve S M, DeLuca A W, Diehl N L, Kermode J C
Department of Pharmacology, College of Medicine, University of Vermont, Burlington 05405.
Peptides. 1992 Sep-Oct;13(5):919-26. doi: 10.1016/0196-9781(92)90050-d.
The molecular weight of the vasoactive intestinal peptide (VIP) receptor was assessed in bovine aorta, and rat liver, lung, and brain by covalent cross-linking and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The receptor in all four tissues was found to be a single polypeptide of approximate M(r) 54,000, contradicting previous claims for substantial heterogeneity in the molecular weight of this receptor. Guanine nucleotides inhibit cross-linking of 125I-VIP to its receptor, and cross-linking with ethylene glycolbis(succinimidylsuccinate) provides further evidence for complex formation between VIP, its receptor and a guanine nucleotide-binding regulatory protein (G-protein). The precise mechanism of receptor-G-protein coupling may differ between the aorta and other tissues.
通过共价交联和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳，评估了牛主动脉、大鼠肝脏、肺和脑中血管活性肠肽（VIP）受体的分子量。发现所有这四种组织中的受体均为一条分子量约为54,000的单一多肽，这与之前关于该受体分子量存在显著异质性的说法相矛盾。鸟嘌呤核苷酸可抑制125I-VIP与其受体的交联，并且用乙二醇双（琥珀酰亚胺琥珀酸酯）进行交联为VIP、其受体和鸟嘌呤核苷酸结合调节蛋白（G蛋白）之间形成复合物提供了进一步的证据。受体与G蛋白偶联的确切机制可能在主动脉和其他组织之间有所不同。
