한국생물공학회:학술대회논문집

The Korean Society for Biotechnology and Bioengineering (한국생물공학회)
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Refolding and Characterization of Recombinant Fusion Ferritin by Gel Filtration Chromatography

  • Kim, Hyoung-Won (Department of Chemical Engineering, Chungnam National University) ;
  • An, Eun-Kyoung (Department of Chemical Engineering, Chungnam National University) ;
  • Shin, Mi-Young (Department of Chemical Engineering, Chungnam National University) ;
  • Kim, In-Ho (Department of Chemical Engineering, Chungnam National University)
  • Published : 2003.10.22
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Abstract

Fusion $ferritin(F_H+F_L),$ an iron-binding protein, was purified from recombinant E. coli by gel filtration chromatography after two-step sonications. Unfolded ferritin was refolded by GFC with various refolding enhancing additives. 50 mM Tris-HCI(pH 7.4) buffers containing 2 M urea and additive was used in GFC. Objective was to characterize the structure change at various conditions. Molecular weight was determined using GF-HPLC and RP-HPLC was used to quantify the unfolded and refolded proteins. Activity was confirmed by iron-uptake reaction.

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