Abstract
ROUTINE chromatography of proteins was made possible by the introduction of cellulose ion-exchangers1. Protein chromatography on ion-exchangers is technically simple but theoretically complex, there being no quantitative theory to act as a guide for experimentation. Proteins are usually unilaterally distributed between the ion-exchange matrix and the surrounding liquid. They are either quantitatively adsorbed (Kd = ∞ : RF = 0) or not at all (Kd = 0 : RF = 1)2. Finite distribution coefficients are seldom obtained and only in well specified conditions. Gradient elution3 is used to make the separation of proteins on ion-exchangers practicable, where the distribution coefficients shift from zero to infinity or vice versa in a concentration interval too narrow to be otherwise adjusted. On the other hand, calculation of the shape and position of the gradient effluent is difficult with present ion-exchange systems, for the gradient is altered continuously during passage through the bed.
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PORATH, J., FRYKLUND, L. Chromatography of Proteins on Dipolar Ion Adsorbants. Nature 226, 1169–1170 (1970). https://doi.org/10.1038/2261169a0
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DOI: https://doi.org/10.1038/2261169a0
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