| Literature DB >> 6329822 |
P Robberecht, M Waelbroeck, P de Neef, J C Camus, A Vandermeers, M C Vandermeers-Piret, J Christophe.
Abstract
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 greater than helodermin greater than secretin greater than 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.Entities:
Mesh：
Substances：
Year: 1984 PMID： 6329822 DOI： 10.1016/0014-5793(84)80872-8
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124