title: Photoaffinity labeling of functional states of the nicotinic acetylcholine receptor.
abstract: The nicotinic acetylcholine receptor was subjected to photoaffinity labeling in different conformational and functional states. The photolabel used was the ion-channel blocker [3H]-TPMP+. A procedure is described for isolating labeled delta-polypeptide chains from the receptor complex by preparative SDS-polyacrylamide gel electrophoresis. The photolabel was localized in the primary structure of the delta-chain. The site of labeling was found to be identical when photoaffinity labeling was performed in the resting, desensitized, or antagonist state, respectively.
authors: Institut für Biochemie, Freie Universität Berlin, West Germany.
authors: W
authors: W
authors: Oberthür
authors: F
authors: F
authors: Hucho
mesh_terms: D000345:Affinity Labels; D000595:Amino Acid Sequence; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D007473:Ion Channels; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011950:Receptors, Cholinergic / Q000378:metabolism*; D014101:Torpedo; D014320:Triphenylmethyl Compounds
chemical_list: D000345:Affinity Labels; D007473:Ion Channels; D011950:Receptors, Cholinergic; D014320:Triphenylmethyl Compounds