Solubilization of adrenal medullary opioid receptors.
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.
Kamikubo
K
K
Third Department of Internal Medicine, Gifu University School of Medicine, Japan.
Murase
H
H
Murayama
M
M
Miura
K
K
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
D011957:Receptors, Opioid; D004072:Digitonin