title: Amphiphilic agarose-based adsorbents for chromatography. Comparative study of adsorption capacities and desorption efficiencies.
abstract: A number of hydrophobic derivatives attached to cross-linked agarose were studied as protein adsorbents. Differences in the adsorption and desorption behaviour were determined as functions of type and concentration of selected salts. Whereas octyl- and phenyl-Sepharose adsorb serum albumin preferentially, pyridyl-S-agarose shows a much stronger preferential affinity for IgG in the presence of high concentrations of lyotropic salts, such as sulphates. In contrast to pyridyl-S-agarose, a large portion of proteins remained fixed to octyl- and phenyl-Sepharose after extensive washing with 1 M NaOH.
authors.affiliation: Biochemical Separation Centre, Uppsala University, Sweden.
authors.forename: S
authors.initials: S
authors.lastname: Oscarsson
authors.forename: D
authors.initials: D
authors.lastname: Angulo-Tatis
authors.forename: G
authors.initials: G
authors.lastname: Chaga
authors.forename: J
authors.initials: J
authors.lastname: Porath
mesh_terms: D000327:Adsorption; D002846:Chromatography, Affinity; D006801:Humans; D007070:Immunoglobulin A / Q000032:analysis; D012492:Salts; D012685:Sepharose; D012709:Serum Albumin / Q000032:analysis
chemical_list: D007070:Immunoglobulin A; D012492:Salts; D012709:Serum Albumin; D012685:Sepharose