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Quantitation of non-ideal behavior in protein size-exclusion chromatography

Authors
Journal
Journal of Chromatography A
0021-9673
Publisher
Elsevier
Publication Date
Volume
635
Issue
1
Identifiers
DOI: 10.1016/0021-9673(93)83113-7
Disciplines
  • Biology
  • Mathematics

Abstract

Abstract The size-exclusion chromatographic partition coefficient ( K sec) was measured on a Superose 6 column for three sets of well-characterized spherically symmetrical solutes: the compact, densely branched non-ionic polysaccharide, Ficoll; the flexible chain non-ionic polysaccharide, pullulan; and compact, anionic synthetic polymers, carboxylated starburst dendrimers. All three solutes display a congruent dependence of K sec on solute radius, R. In accord with a simple geometric model for SEC, all of these data conform to the same linear plot of K SEC 1/2 vs. R. This plot reveals the behavior of non-interacting spheres on this column. Comparison of results for a number of globular proteins at various pH values to this “ideal” curve allows a quantitative measure of protein attraction or repulsion. It is shown that the usual procedure of obtaining a “best-fit” curve for a set of proteins is likely to generate an erroneous calibration curve.

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