Chromatographic preparation and in vitro properties of albumin from human plasma.

Abstract

Albumin has been purified by chromatography using standardized procedures with different starting materials depending on previous fractionation. Plasma can be used directly after cryoprecipitation and Factor IX adsorption or after isolation of IgG. The plasma was centrifuged and then desalted on Sephadex G-25 Coarse, the pH was adjusted, and the euglobulins were precipitated before ion-exchange chromatography on DEAE- and CM-Sepharose CL-6B. This was followed by concentration by ultrafiltration, gel filtration on Sephacryl S-200, and final concentration and formulation. The albumin obtained was 99% pure and contained less than 1% of aggregated protein.