Ion-exchange Chromatography Of Proteins Research Articles

Chromatofocusing: Isoelectric focusing on ion-exchange columns : II. Experimental verification

The focusing effects in the ion-exchange chromatography of proteins in a pH gradient predicted in Part I have been confirmed experimentally. Each protein seeks its own position in the pH gradient. The separations obtained are similar to those in the preparative electrophoretic method. Donnan potentials, under conditions approximating to those in ion-exchange columns, were determined by employing 24Na + as a probe. Utilizing these values, the observed phenomena could be understood in terms of the equations calculated for the width of the protein bands and for the pH of the emerging protein solutions.

High speed ion exchange chromatography of proteins.

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTHigh speed ion exchange chromatography of proteinsShung-Ho. Chang, Rodney. Noel, and Fred E. RegnierCite this: Anal. Chem. 1976, 48, 13, 1839–1845Publication Date (Print):November 1, 1976Publication History Published online1 May 2002Published inissue 1 November 1976https://doi.org/10.1021/ac50007a008RIGHTS & PERMISSIONSArticle Views491Altmetric-Citations99LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (854 KB) Get e-Alerts Get e-Alerts

Ion exchange chromatography of proteins. Artifact separations resulting from inadequate pH control.

Abstract The ion exchange chromatography of wheat proteins on carboxymethyl cellulose is described. As the concentration of buffer in the eluant is reduced, a higher concentration of sodium ion is required to elute a give protein component; and concurrently the pH of the eluant is observed to deviate from the original pH of the eluant. It is suggested that these effects are related and that they arise from the ion exchange process itself as a result of the non equivalence of eluant ions and charged protein groups. The general conclusion that eluant solutions for protein ion exchange chromatography should be effectively buffered to reduce the possibility of artifact separations also appears to apply to chromatography with DEAE cellulose and the other adsorbents.