Abstract
2-Aminoethyl p-nitrophenyl methylphosphonate, a potential inhibitor of acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7), was coupled to extended sepharose, thus forming covalent affinity support for purification of acetylcholinesterase. Cholinesterase from electric eel was trapped on the column by forming a covalent bond with the insoluble matrix. The enzyme was recovered from the column in very good quality by using the reactivator 2-(hydroximinomethyl)-1-methylpyridinium iodide (2PAM) or 1,1′-trimethylene bis(4-hydroximinomethyl pyridinium) dibromide (TMB 4) . The column functioned as a covalent affinity column for eel cholinesterase and α-chymotrypsin (EC 3.4.4.5).
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