Enrichment of proteinaceous materials on a strong cation-exchange diol silica restricted access material: protein-protein displacement and interaction effects

Journal of Chromatography. a
Olga WillemsenKlaus K Unger

Abstract

A study of size exclusion and enrichment of proteins employing strong cation-exchange diol silica restricted access material (SCX-RAM) under saturation conditions is presented. Experiments were carried out with bacitracin, protamine, ribonuclease, lysozyme and bovine serum albumin as individual proteinaceous analytes as well as comprehensive binary mixtures and with human urine samples. Protein size dependent capacity features of the SCX-RAM column was observed. Bacitracin demonstrated the highest capacity followed by protamine while adsorption capacities of both ribonuclease and lysozyme were found smaller by a factor of 10. Applying binary protein samples occurring displacement effects were apparent: proteins with strong cationic properties displaced those already adsorbed by the bonded cation-exchange ligands. Bacitracin was displaced in all binary mixture experiments in particular by protamine. Furthermore, the binary mixtures displayed increased adsorption for some proteins due to complex formation. Lysozyme and ribonuclease showed double capacity values when paired with bacitracin. Both phenomena, displacement and enhanced adsorption occurred in the saturated state and led to changes in the urine composition during sample...Continue Reading

Citations

Mar 17, 2010·Angewandte Chemie·Klaus K UngerR Skudas
Jun 19, 2004·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Eiichi YamamotoNaoki Asakawa
Nov 23, 2006·Journal of Biochemical and Biophysical Methods·Wayne M Mullett
Dec 29, 2011·Journal of Biomedicine & Biotechnology·Inez FinoulstPeter Verhaert
Dec 22, 2012·Se pu = Chinese journal of chromatography·Xiaoyu WuXianhua Wang

Related Concepts

Cation Exchange Resins
Polypeptides
Gene Products, Protein
Proteinuria
Quso G-32

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