We have previously shown that the diphtheria toxin variant CRM197 (cross-reacting material 197) can be overexpressed in Escherichia coli at high levels, yielding insoluble aggregates, which were solubilized using urea. This study reports a comparison of three matrices suitable for the purification and refolding of recombinant CRM197 by metal-chelating affinity chromatography. Moreover, we show that refolded CRM197 features enzymatic activity.

On-column refolding of diphtheria toxin variant CRM197 by different metal-chelating affinity chromatography matrices / Alessandra Stefan; Mattia Boiani; Luca Longanesi; Alejandro Hochkoeppler. - In: JOURNAL OF CHEMISTRY AND CHEMICAL ENGINEERING. - ISSN 1934-7375. - STAMPA. - 8:(2014), pp. 1135-1141. [10.17265/1934-7375]

On-column refolding of diphtheria toxin variant CRM197 by different metal-chelating affinity chromatography matrices

STEFAN, ALESSANDRA;HOCHKOEPPLER, ALEJANDRO
2014

Abstract

We have previously shown that the diphtheria toxin variant CRM197 (cross-reacting material 197) can be overexpressed in Escherichia coli at high levels, yielding insoluble aggregates, which were solubilized using urea. This study reports a comparison of three matrices suitable for the purification and refolding of recombinant CRM197 by metal-chelating affinity chromatography. Moreover, we show that refolded CRM197 features enzymatic activity.
2014
On-column refolding of diphtheria toxin variant CRM197 by different metal-chelating affinity chromatography matrices / Alessandra Stefan; Mattia Boiani; Luca Longanesi; Alejandro Hochkoeppler. - In: JOURNAL OF CHEMISTRY AND CHEMICAL ENGINEERING. - ISSN 1934-7375. - STAMPA. - 8:(2014), pp. 1135-1141. [10.17265/1934-7375]
Alessandra Stefan; Mattia Boiani; Luca Longanesi; Alejandro Hochkoeppler
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/425171
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