Abstract
The charge characteristics of a number of proteins were determined over a broad range of pH using the “electrophoretic titration” technique recently introduced by Rosengren and others. The chromatographic behavior of these proteins was then characterized by cation- and anion-exchange chromatography to determine if electrophoretic and chromatographic characteristics could be correlated. The results indicate that retention, in terms of salt concentration required for elution, is generally dependent upon the charge density of a protein. Exceptions to this dependence were found, and most of these exceptions were probably due to asymmetry in shape, or charge inhomogeneity within the protein.
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