ADSORPTION BEHAVIOR OF SOME PROTEINS ON THE TSK-DEAE5PW ANION-EXCHANGER

The adsorption isotherms of conalbumin, myoglobin, and gamma-globulin on TSK-DEAE 5PW are determined by frontal analysis using buffer solutions of different ionic strengths. The data are well accounted for by a bi-Langmuir isotherm model, corresponding to two types of adsorption sites with different adsorption energies. The column saturation capacity varies considerably from one protein to the other and for a given compound, depends strongly on the ionic strength of the mobile phase. This demonstrates that the composition of the mobile phase used in preparative liquid chromatography must be chosen carefully, to optimize the combined effect of the relative retention and of the column saturation capacity on the production rate, not either one of these factors.