Experimental and numerical studies of the chromatofocusing of dilute proteins using retained pH gradients formed on a strong-base anion-exchange column

Journal of Chromatography. a
J C Strong, Douglas D Frey

Abstract

The separation of dilute protein mixtures was achieved using simple monovalent buffering species to form retained, internally produced pH gradients on a strong-basic anion-exchange column. Highly focused proteins bands localized on stepwise pH transitions were produced experimentally under trace and volume overloaded feed conditions. Numerical simulations were performed that accurately predict the pH profile and protein band shapes in the column effluent. Experimental results were combined with numerical investigations to explore strategies for designing efficient preparative-scale chromatofocusing systems using simple, inexpensive buffers and adsorbents.

Citations

Nov 30, 2002·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·David M LubmanTimothy J Barder
Jul 27, 2010·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Sascha HagemannRichard Dodel
Jun 30, 2009·Journal of Chromatography. a·Anna Rozhkova
Apr 15, 2008·Journal of Chromatography. a·Hyeyeung Kim, David M Lubman
Jul 29, 2006·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Karin Ahrer, Alois Jungbauer
Jul 10, 2007·Analytical Biochemistry·Ziad J SahabQing-Xiang Amy Sang
Jun 10, 2004·American Journal of Physiology. Lung Cellular and Molecular Physiology·Jan HirschMichael A Matthay
Apr 23, 2008·Current Protocols in Protein Science·Kan ZhuTimothy J Barder

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