Separation and Purification of Recombinant Human Serum Albumin by Ion Exchange Chromatography

Adsorption and elution characteristics of human serum albumin (HSA) and recombinant HSA under different operation conditions, such as pH, ionic strength of buffer solution, flow rate and concentration of feed were investigated in fixed bed chromatography with three kinds of anion exchange gel beads as supports. Separation of HSA and ovalbumin in chromatography was studied. Selectivity between recombinant human serum albumin and hybrid proteins by anion exchange chromatography were discussed. It was experimentally shown that high resolution and recovery of recombinant HSA were obtained in fixed bed chromatography with DEAE Sepharose FF as support.