Purification of acetylcholinesterase from pig cerebral cortex by affinity chromatography.

Acetylcholinesterase from pig cerebral cortex was solubilised with 1% (w/v) Triton X-100 and purified by affinity chromatography. Three different ligands were investigated and details are given for their preparation. The elution profile depended on the presence of Triton X-100, the ionic strength and the inhibitor used to remove the enzyme from the column as well as the nature of the affinity material. The most efficient purification was obtained when the enzyme was eluted from a column containing the acetylcholinesterase inhibitor [1-methyl-9-(Nbeta-epsilon-amino-caproyl)-beta-aminopropylamino] acridinium bromide hydrobromide covalently linked to Sepharose 4B. A recovery of 44% of the applied enzyme was eluted from the column with a specific activity of 148 mumoles min-1 mg-1 and a purification of 900-fold.