[Effective binding of alpha-bungarotoxin with the solubilized alpha-subunit of Torpedo californica acetylcholine receptor].

alpha-Subunit of the Torpedo californica nicotinic acetylcholine receptor was isolated by preparative SDS-PAGE followed by reversed-phase HPLC on a C4 column in an acetonitrile-isopropanol gradient in water. After removal of the organic solvents and solubilization in beta-octylglucoside, the purified alpha-subunit binds alpha-bungarotoxin with high affinity (Kd 28 nM).