title: Hydrophobic interaction chromatography of proteins. I. Comparison of selectivity.
abstract: Currently, the selection of a hydrophobic interaction chromatography (HIC) sorbent for protein separation purposes is entirely based on empirical means. An attempt was made to characterize different HIC sorbents from various manufacturers. The selectivity was determined by isocratic pulse experiments of a set of reference proteins and an algorithm was developed to classify the sorbents according to their selectivity and hydrophobicity. The obtained semi-quantitative parameters take into account the dependence of salt on adsorption. The sorbent characteristics evaluated with the model proteins were compared to the separation of a real feedstock. A good agreement was achieved between the developed evaluation procedure and the separation behaviour of the real feed stock.
authors.affiliation: Institute for Applied Microbiology, University of Agricultural Sciences, Vienna, Austria.
authors.forename: Christine
authors.initials: C
authors.lastname: Machold
authors.forename: Karin
authors.initials: K
authors.lastname: Deinhofer
authors.forename: Rainer
authors.initials: R
authors.lastname: Hahn
authors.forename: Alois
authors.initials: A
authors.lastname: Jungbauer
mesh_terms: D002853:Chromatography, Liquid / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D011506:Proteins / Q000302:isolation & purification*; D012680:Sensitivity and Specificity
chemical_list: D011506:Proteins