title: Study of conformational effects of recombinant interferon gamma adsorbed on a non-porous reversed-phase silica support.
abstract: Reversed-phase chromatography is a powerful method for separating recombinant interferon gamma and one of its analogues differing only by a single amino acid residue. Structural differences of the proteins explain this separation ability as demonstrated from adsorption studies on a non-porous reversed-phase support. To reveal the structural differences occurring in the adsorbed state, two different and independent methods were employed. The variation of the retention with the slope of the linear gradient gave information about the molecular contact area of the protein with the support. For different experimental conditions, these data were correlated with the adsorbent capacities measured on an n-octadecyl-modified non-porous silica support. These supports are useful for these types of experiments because the protein is adsorbed exclusively at the external surface of the beads. Moreover, a small amount of protein is necessary to saturate the column, owing to its low capacity.
authors.affiliation: Laboratoire de Physico-Chimie des Biopolymères, UMR 27, CNRS-Université Paris Val de Marne, Thiais, France.
authors.forename: B
authors.initials: B
authors.lastname: de Collongue-Poyet
authors.forename: C
authors.initials: C
authors.lastname: Vidal-Madjar
authors.forename: B
authors.initials: B
authors.lastname: Sebille
authors.forename: K K
authors.initials: KK
authors.lastname: Unger
mesh_terms: D000327:Adsorption; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D006801:Humans; D007371:Interferon-gamma / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D012822:Silicon Dioxide; D013696:Temperature
chemical_list: D011994:Recombinant Proteins; D012822:Silicon Dioxide; D007371:Interferon-gamma