A Chromatographic Procedure for the Purification of Human Plasma Albumin

Abstract
Albumin is obtainable from human blood plasma by an ion exchange chromatographic procedure in a yield of about 95% and a purity well above Pharmacopoeia requirements. Cryosupernatant, factor IX depleted plasma is precipitated with 12 and 25% wt/vol polyethylene glycol 4000. The 2nd precipitate is dissolved to 8% wt/vol protein and applied to a DEAE-Sephadex A-50 or a DEAE-Sepharose CL-6B column. Albumin is further purified by chromatography on SP-Sephadex C-50. Gel filtration on Sephadex G-25 is used for desalting prior to lyophilization. The process was initially designed for fractionation of 50 l plasma/wk but can be further scaled up to meet considerably higher capacity requirements.