Acetylcholinesterase: Differential affinity chromatographic purification of 11 S and 18 S plus 14 S forms; the importance of multiple-site interactions and salt concentration

A revised synthesis of 10-methyl-9-[Nβ-(6-aminohexanoyl)-β-aminopropylamino]acridinium-Sepharose 2B is presented. Conditions for the individual purification of either 11 S (globular) or 18 S plus 14 S (asymmetric) acetylcholinesterase are described and the selective purification of either 11 S or 18 S plus 14 S enzyme from mixtures of the species is shown to be possible. The mechanism resulting in selective purification is discussed and the postulate that multiple-site interaction takes place between enzyme and immobilized ligand is presented.