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Acetylcholinesterase from rat brain was solubilized with 1% (w/v) Triton X-100 and purified by affinity chromatography. Two different ligands were investigated. The most efficient purification was obtained when the enzyme was eluted from a column containing the acetylcholinesterase inhibitor N-methyl-3-aminopyridinium iodide covalently linked to Sepharose 2B. An initial recovery of 6% of the applied enzyme increased to 70% after treatment with Amberlite CG-120. The partially purified enzyme had a specific activity of 205 mumoles min-1 mg-1 and a purification of 162-fold with respect to the brain homogenate and 44-fold with respect to the Triton solubilized enzyme. The effect of metal cations on the stability of the partially purified enzyme during storage at --20 degrees C was also investigated. The addition of MgCl2 to the purified enzyme prevented the rapid loss of enzyme activity.


C J Vidal, E Elmi-Akhounie, M S Chai, D T Plummer. Affinity chromatography of acetylcholinesterase. The use of Amberlite CG-120 for dissociating the enzyme-inhibitor complex. Journal of chromatography. 1981 Nov 27;219(1):71-9

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PMID: 7320131

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