Molecular orientation of immunoglobulin G at high concentration on an ion-exchange sorbent.
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.
Mazsaroff
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I
Department of Biochemistry, Purdue University, West Lafayette, IN 47907.
Cook
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S
Regnier
F E
FE
D000327:Adsorption; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002852:Chromatography, Ion Exchange; D007074:Immunoglobulin G / Q000302:isolation & purification*; D013816:Thermodynamics
D007074:Immunoglobulin G