Physical characterization of native opiate receptors. Additional information from detailed binding analysis of a radiation-inactivated receptor.
Target size analyses of the etorphine receptor were performed on frozen rat brain P2 homogenates using the radiation inactivation technique. Multi-point saturation curves at each radiation dose revealed that the apparent dissociation constant for the binding of this ligand to its receptor is a function of the dose. Analysis of the results shows clearly that the ligand-binding macromolecule is functionally coupled to at least one other macromolecule. When the coupling is destroyed the ligand dissociation constant becomes larger by over an order of magnitude. Thus, the variation of the dissociation constant with dose yields interesting new information on the nature of the native receptor which has implications with respect to the conformation of the binding site and to solubilization and cloning methods directed towards sequencing the ligand-binding component of opiate receptors.
D000818:Animals; D005048:Etorphine / Q000378:metabolism; D008297:Male; D008433:Mathematics; D008954:Models, Biological; D011487:Protein Conformation; D051381:Rats; D011919:Rats, Inbred Strains; D011957:Receptors, Opioid / Q000032:analysis* / Q000528:radiation effects
D011957:Receptors, Opioid; D005048:Etorphine