par Robberecht, Patrick 
;Waelbroeck, Magali ;De Neef, Philippe ;Camus, Jean Claude ;Vandermeers, André ;Vandermeers-Piret, Marie-Claire ;Christophe, Jean
Référence FEBS letters, 172, 1, page (55-58)
Publication Publié, 1984-06
;Waelbroeck, Magali ;De Neef, Philippe ;Camus, Jean Claude ;Vandermeers, André ;Vandermeers-Piret, Marie-Claire ;Christophe, Jean Référence FEBS letters, 172, 1, page (55-58)
Publication Publié, 1984-06
Article révisé par les pairs
| Résumé : | 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. |
