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  • Title: Specific labelling by [125I]helodermin of high-affinity VIP receptors in rat liver membranes.
    Author: Robberecht P, Waelbroeck M, de Neef P, Camus JC, Vandermeers A, Vandermeers-Piret MC, Christophe J.
    Journal: FEBS Lett; 1984 Jun 25; 172(1):55-8. PubMed ID: 6329822.
    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.
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