Affinity chromatography and affinity partition of human serum pre-albumin using immobilized Remazol Yellow GGL. Evidence that albumin increases binding of pre-albumin to the dye

Abstract

Pre-albumin was isolated from human serum or plasma by ammonium sulphate fractionation and by chromatography on dye-substituted Sephadex G-100 to a high degree of purity. The interaction of the pre-albumin with the dye Remazol Yellow GGL was studied in more detail by means of affinity partitioning in an aqueous two-phase system composed of dextran and poly(ethylene glycol). In the presence of dye-substituted poly(ethylene glycol) the partition coefficient of pre-albumin increases, indicating an interaction with the dye. Human serum albumin was found to enhance this interaction considerably. A similar effect was also shown by bovine albumin but not by egg albumin.