Characterization, solubilization and purification of an opioid receptor from the brain of the frog Rana ridibunda.
The brain of the frog R. ridibunda contains a major opioid binding site which in vitro pharmacological profile is different from those of mammalian mu, delta- and kappa-opioid sites. In digitonin extracts, this major opioid site exists as two molecular forms -10S and 12S- which are clearly resolved by sedimentation in sucrose gradients and which are thought to represent the opioid receptor alone (10S) or associated (12S) with a guanine nucleotide regulatory protein. Purification of the digitonin extracts by affinity chromatography on immobilized dynorphin, results in a single major protein component of apparent Mr approximately 64,000.
Pascaud
A
A
Laboratoire de Pharmacologie et de Toxicologie Fondamentales CNRS, Toulouse, France.
Mollereau
C
C
Puget
A
A
Baillat
G
G
Mazarguil
H
H
Meunier
J C
JC
D000818:Animals; D001921:Brain / Q000378:metabolism*; D004174:Diprenorphine / Q000378:metabolism; D005048:Etorphine / Q000378:metabolism; D007700:Kinetics; D011895:Rana ridibunda; D011957:Receptors, Opioid / Q000302:isolation & purification* / Q000378:metabolism; D012995:Solubility
D011957:Receptors, Opioid; D004174:Diprenorphine; D005048:Etorphine