Purification of phospholipase-C from Bacillus cereus by affinity chromatography on 2-(4-aminophenylsulphonyl)ethyl-cellulose.

A new method for the purification of phospholipase-C (phosphatidylcholine cholinephosphohydrolase, EC 3.1.4.3) from Bacillus cereus has been developed, based on its affinity to 2-(4-aminophenylsulphonyl)ethyl derivative of beaded cellulose. The enzyme was adsorbed on the affinity sorbent through a site(s) that was clearly distinct from its catalytically active site, because it was still active in the immobilized state. A possible role of enzyme-inhibitor interaction in enzyme binding to the ligand used is discussed.