Son_2002_Int.J.Biochem.Cell.Biol_34_204

The purification of a soluble acetylcholinesterase from Japanese quail brain using affinity chromatography on concanavalin A-Sepharose and edrophonium-Sepharose is described The affinity matrix was synthesized by coupling an inhibitor edrophonium to epoxy-activated Sepharose Acetylcholinesterase was purified 10416-fold with a specific activity of 2500 U/mg protein Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and mercaptoethanol gave only one band with a molecular weight of 62.5 kDa The molecular weight of the purified acetylcholinesterase was estimated to be 245.5 kDa by gel chromatography on Sephacryl S-200 under nondenaturing conditions Based on the molecular weight obtained by both SDS-PAGE and gel filtration the purified acetylcholinesterase was assumed to be a tetrameric form