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作 者:Alessandra Stefan Mattia Boiani Luca Longanesi Alejandro Hochkoeppler
机构地区:[1]Department of Pharmacy and Bioteehnology, University of Bologna, Bologna 4, 40136, Italy [2]CSGI (Center for Colloid and Surface Science), Department of Chemistry, University of Firenze, Sesto Fiorentino 3, 50019, ltaly
出 处:《Journal of Chemistry and Chemical Engineering》2014年第12期1135-1141,共7页化学与化工(英文版)
摘 要:We have previously shown that the diphtheria toxin variant CRM 197 (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.
关 键 词:REFOLDING chromatographic matrix cross-reacting material 197 metal-chelating affinity chromatography
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