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Affinity chromatography and affinity partition of human serum pre‐albumin using immobilized remazol yellow GGL
Author(s) -
Birkenmeier G.,
Tschechonien B.,
Kopperschläger G.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81097-2
Subject(s) - chromatography , chemistry , bovine serum albumin , ethylene glycol , albumin , sephadex , human serum albumin , peg ratio , affinity chromatography , serum albumin , dextran , partition coefficient , human albumin , polyethylene glycol , ammonium , biochemistry , organic chemistry , finance , economics , enzyme
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