title: Purification of soluble acetylcholinesterase from Japanese quail brain by affinity chromatography.
abstract: 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 10,416-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.
authors.affiliation: Department of Biology, Dongguk University, Seoul 100-715, South Korea.
authors.forename: Ji Young
authors.initials: JY
authors.lastname: Son
authors.forename: Sook
authors.initials: S
authors.lastname: Shin
authors.forename: Kwang Ho
authors.initials: KH
authors.lastname: Choi
authors.forename: In Kook
authors.initials: IK
authors.lastname: Park
mesh_terms: D000110:Acetylcholinesterase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002846:Chromatography, Affinity / Q000379:methods*; D002850:Chromatography, Gel; D003370:Coturnix / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight
chemical_list: D000110:Acetylcholinesterase