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Molecular orientation of immunoglobulin G at high concentration on an ion-exchange sorbent
I Mazsaroff1, S Cook, F E Regnier
1Department of Biochemistry, Purdue University, West Lafayette, IN 47907.
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.
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.