FEBS Letters | |
Specific labelling by [125I]helodermin of high‐affinity VIP receptors in rat liver membranes | |
Vandermeers, André1  Vandermeers-Piret, Marie-Claire1  Christophe, Jean1  De Neef, Philippe1  Waelbroeck, Magali1  Camus, Jean-Claude1  Robberecht, Patrick1  | |
[1] Department of Biochemistry and Nutrition, Medical School, Université Libre de Bruxelles, Bid de Waterloo 115, B-1000 Brussels, Belgium | |
关键词: Gila Monster venom Helodermin Vasoactive intestinal peptide Secretin Growth hormone releasing factor Adenylate cyclase Rat liver membrane; VIP; vasoactive intestinal peptide; GRF; growth hormone releasing factor; PHI; porcine peptide having N-terminal histidine and C-terminal isoleucineamide; hpGRF; human pancreatic growth hormone releasing factor; | |
DOI : 10.1016/0014-5793(84)80872-8 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Helodermin, a newly isolated peptide from Gila Monster venom, is structurally related to VIP and secretin. When used as radioligand, [125I]helodermin bound rapidly and reversibly to crude rat liver membranes, the dissociation being accelerated by GTP. Competition binding curves of [125I]helodermin and [125I]VIP with unlabelled peptides showed the following order of decreasing affinity: VIP > helodermin > secretin > hpGRF(1–29)-NH2. The shape of binding curves and of concurrent adenylate cyclase activation is compatible with the specific labelling, by [125I]helodermin, of a class of high-affinity VIP receptors that is capable to stimulate adenylate cyclase.
【 授权许可】
Unknown
【 预 览 】
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