title: Solubilization of adrenal medullary opioid receptors.
abstract: The opioid-binding activity of digitonin extract of bovine adrenal medullary membranes was studied. [3H]Diprenorphine binding to the solubilized material was rapid and saturable. The dissociation constant of [3H]diprenorphine binding was 0.76 nM. Several opioids displaced the [3H]diprenorphine binding. The complex of [3H]diprenorphine and the solubilized binding sites was eluted as a single peak on a Sepharose 6B column and showed an apparent molecular weight of 200,000. These results indicate that active opioid receptors are solubilized with digitonin from bovine adrenal medullary membranes.
authors.affiliation: Third Department of Internal Medicine, Gifu University School of Medicine, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Kamikubo
authors.forename: H
authors.initials: H
authors.lastname: Murase
authors.forename: M
authors.initials: M
authors.lastname: Murayama
authors.forename: K
authors.initials: K
authors.lastname: Miura
mesh_terms: D000313:Adrenal Medulla / Q000032:analysis* / Q000187:drug effects; D000818:Animals; D002417:Cattle; D002499:Centrifugation, Density Gradient / Q000379:methods; D004072:Digitonin / Q000494:pharmacology; D011957:Receptors, Opioid / Q000648:ultrastructure*; D012995:Solubility
chemical_list: D011957:Receptors, Opioid; D004072:Digitonin