title: Molecular orientation of immunoglobulin G at high concentration on an ion-exchange sorbent.
abstract: The change of molecular orientation of IgG, bound on a strong-anion-exchange surface, was studied using a generalization of the stoichiometric displacement model, over the entire range of protein adsorption isotherms. The Z number was found to decrease with increasing stationary phase protein concentration, approaching a limiting value. The analogy of the multiple equilibria model within highly cooperative identical binding sites was suggested as a possible way to evaluate the observed change in Z number with the protein concentration.
authors.affiliation: Department of Biochemistry, Purdue University, West Lafayette, IN 47907.
authors.forename: I
authors.initials: I
authors.lastname: Mazsaroff
authors.forename: S
authors.initials: S
authors.lastname: Cook
authors.forename: F E
authors.initials: FE
authors.lastname: Regnier
mesh_terms: D000327:Adsorption; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002852:Chromatography, Ion Exchange; D007074:Immunoglobulin G / Q000302:isolation & purification*; D013816:Thermodynamics
chemical_list: D007074:Immunoglobulin G