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.
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.
D000645:Ammonium Sulfate; D000818:Animals; D001391:Azo Compounds; D002417:Cattle; D002645:Chickens; D002846:Chromatography, Affinity / Q000379:methods; D006801:Humans; D010047:Ovalbumin / Q000302:isolation & purification; D011228:Prealbumin / Q000302:isolation & purification* / Q000378:metabolism; D012709:Serum Albumin / Q000302:isolation & purification / Q000378:metabolism; D012710:Serum Albumin, Bovine / Q000302:isolation & purification
D001391:Azo Compounds; D011228:Prealbumin; D012709:Serum Albumin; C035187:reactive yellow 13; D012710:Serum Albumin, Bovine; D010047:Ovalbumin; D000645:Ammonium Sulfate