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[Immobilized Ni(2+)-IDA metal chelating affinity membrane chromatography for purification of commercial human serum albumin].

Further purification of commercial human serum albumin was studied on immobilized Ni(2+)-IDA composite membrane cartridge. Effect of pH on HSA binding capacity was examined. A lot of impurities in the commercial HSA had been removed by a single step purification with a recovery of more than 85% of the protein bound on membrane cartridge. The purified HSA was of comparable purity of that from Sigma company analyzed by capillary electrophoresis. The nickel ion retained in the protein solution could be removed efficiently with the N, N, N'-tris (carboxymethyl) ethylenediamine chelating membrane cartridge.