Cholinergic binding proteins were purified from torpedo electric organ. The preparation comprises: solubilization by non-ionic detergents followed by unspecific prepurification. For prepurification the double reversed technique proved to be very useful. Finally we applied affinity chromatography. For the affinity purification we used resins with chemically well defined small ligand groups from the depolarizing type (carbachol- and decamethonium-analogue), and from the stabilizing type (gallamine amide amine). The purified receptor proteins from all three resins showed different subunit compositions and different properties of alpha-bungarotoxin binding.