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  • Title: Distinct molecular forms of opiate binding in the frog brain.
    Author: Puget A, Jauzac P, Meunier JC.
    Journal: Life Sci; 1983; 33 Suppl 1():199-202. PubMed ID: 6319860.
    Abstract:
    In frog brain membranes, equilibrium saturation binding of the opiate agonist: 3H-etorphine and of the opiate antagonist: 3H-diprenorphine is biphasic. In the presence of sodium ions (120 mM), "kinetic conversions" (unchanged Bmax) are observed: high affinity binding of the 3H-agonist is decreased while high affinity binding of the antagonist is increased. Frog brain membranes were labelled either with 3H-etorphine or with 3H-diprenorphine and solubilized with digitonin. The soluble extracts were centrifuged in sucrose gradients: two distinct components were labelled which sedimented respectively faster (approximately 12 S) and slower (approximately 10 S) than did catalase, used as marker. Pre-incubation of membrane and of 3H-ligand in the presence of 120 mM NaCl resulted in 1) considerably reduced recovery of the 12 S component in labelled form and 2) substantially enhanced labelling of the 10 S component with the 3H-antagonist. Gpp(NH)p (guanyl-5'-yl imidodiphosphate) exerted similar effects as did sodium ions. Taken together, these data suggest that the two components in question represent physically distinct agonist and antagonist forms of frog brain opiate receptors.
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