Abstract
The retention behavior of five globular proteins (ribonuclease, lysozyme, β-lactoglobulin, serum albumin, γ-globulin) was determined on Superose 6 in low ionic strength (0.02–0.04 M) mobile phases of high, intermediate and low pH (10.0, 7.0, 4.3). Quantitative assessments of attractive or repulsive solute-packing interactions were made by comparing the chromatographic partition coefficient to the value obtained for non-interacting spherical solutes on the same column. The dependence of this “non-ideal” adsorption or exclusion on net protein charge is complex, but not very sensitive to protein type. The results suggests that on size-exclusion chromatography packings that behave as weak cation-exchange resins the electrostatic solute-packing interaction is not governed by a highly localized set of a few charged sites.
Published Version
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