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.