Reconstitution of active acetylcholine receptor by hybridisation of binding site-blocked with ion channel-blocked acetylcholine receptor protein.
The nicotinic acetylcholine receptor regulates the ion permeability of the postsynaptic membrane. This report presents evidence that the transmitter binding site and the ion channel may be located on distinct subunits. By hybridisation of receptor complexes, in which the transmitter binding site was blocked with complexes in which the ion channel was irreversibly inhibited, we reconstituted active acetylcholine receptor complexes. The reconstituted system was similar to the native receptor in its ability to regulate the ion permeability of lipid vesicles in response to nicotinic cholinergic effectors.
D000109:Acetylcholine / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002038:Bungarotoxins / Q000494:pharmacology; D002463:Cell Membrane Permeability / Q000187:drug effects; D004557:Electric Organ / Q000378:metabolism; D005399:Fishes / Q000378:metabolism; D066298:In Vitro Techniques; D007473:Ion Channels / Q000187:drug effects / Q000378:metabolism*; D008956:Models, Chemical; D011797:Quinacrine Mustard / Q000494:pharmacology; D011950:Receptors, Cholinergic / Q000378:metabolism*; D011978:Receptors, Nicotinic / Q000378:metabolism*; D012964:Sodium / Q000378:metabolism
D002038:Bungarotoxins; D007473:Ion Channels; D011950:Receptors, Cholinergic; D011978:Receptors, Nicotinic; D011797:Quinacrine Mustard; D012964:Sodium; D000109:Acetylcholine