Use of a snake venom toxin to characterize the cholinergic receptor protein.
alpha-Bungarotoxin, a polypeptide of mol wt 8000 purified from the venom of Bungarus multicinctus, blocks irreversibly and specifically the excitation by cholinergic agonists on the isolated electroplax and on purified membrane fragments in vitro. The toxin also blocks the in vitro binding of decamethonium to a protein recently isolated from electric tissue. This observation strengthens our earlier conclusion that this protein is the cholinergic receptor macromolecule.
D000818:Animals; D002628:Chemoreceptor Cells / Q000187:drug effects*; D003650:Decamethonium Compounds / Q000494:pharmacology; D004524:Eels; D004557:Electric Organ / Q000187:drug effects; D008566:Membranes / Q000187:drug effects; D008970:Molecular Weight; D010277:Parasympathomimetics / Q000037:antagonists & inhibitors*; D010455:Peptides / Q000302:isolation & purification; D011485:Protein Binding / Q000187:drug effects*; D012911:Snakes; D014688:Venoms / Q000494:pharmacology*
D003650:Decamethonium Compounds; D010277:Parasympathomimetics; D010455:Peptides; D014688:Venoms