Partial purification and characterisation of an acetylcholine receptor with nicotinic properties from the supraoesophageal ganglion of the locust (Schistocerca gregaria).

An alpha-bungarotoxin-binding component has been partially purified from the supraoesophageal ganglion of the locust, (Schistocerca gregaria). The component binds alpha-bungarotoxin with a Kd of about 1.7 nM and this value changes little throughout the purification procedure. The specific binding activity ranges from 1.18 pmol alpha-bungarotoxin bound/mg protein for the membrane-bound site up to a maximum of 230 pmol bound/mg protein for the partially purified component. The pharmacological properties of the membrane-bound site are predominantly nicotinic. Affinity labelling of the binding species with 4-(N-maleimido)-[3H]benzyltrimethylammonium suggests that the binding is associated with a peptide of Mr 58000. Polyacrylamide gel electrophoresis of the partially purified of binding component shows three major bands corresponding to Mr of 60000, 41000 and 25000. We suggest that the binding component can be tentatively identified as a nicotinic acetylcholine receptor.