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• W2016077305 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." @default.
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• W2016077305 date "2002-02-01" @default.
• W2016077305 modified "2023-10-18" @default.
• W2016077305 title "Purification of soluble acetylcholinesterase from Japanese quail brain by affinity chromatography" @default.
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• W2016077305 doi "https://doi.org/10.1016/s1357-2725(01)00082-6" @default.
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