The Use of Affinity Gels for the Study of the Ligand Binding Properties of Mammalian Acetylcholinesterase

An affinity adsorption technique for the analysis of the binding sites of acetylcholinesterase for small ligands is presented. By studying the interaction of decamethonium and edrophonium the second anionic binding site of decamethonium ds characterized as having affinity for trimetyl-(p-aminophenyl)ammonium-CH- Sepharose 4B but not for trimethyl-(m-aminophenyl)ammonium- CH-Sepharose 4B. The directional localization of a hydrophobic binding area in the vicinity of the anionic subsite of the catalytic site is tentatively defined