Overexpression, isolation and purification of functionally active bacterioferritin Dps E.coli

Authors

  • Viktoria O. Pokusaeva Мaster’s student, Department of biophysics and biotechnology, Voronezh State University, Voronezh, e-mail: pokusaevavika@mail.ru
  • Sergei S. Antipov PhD in biology, Department of biophysics and biotechnology, Voronezh State University, Voronezh
  • Uliana S. Shvyreva PhD student, Pushchino State natural-scientific Institute, Pushchino, Moscow Region, Department of Functional genomics and cellular stress, Institute of cell biophysics of Russian academy of sciences, Pushchino, Moscow Region
  • Maria N. Tutukina PhD in biology, Department of Functional genomics and cellular stress, Institute of cell biophysics of Russian academy of sciences, Pushchino, Moscow Region, Pushchino State Institute of natural sciences, Pushchino

Keywords:

Escherichia coli, bakterioferritin Dps, DNA, chromatography.

Abstract

A method for isolation and purification of the recombinant Dps protein from Escherichia coli
was suggested. The procedure involves cloning of the dps gene into the pGEM vector, followed by the
induction of the recombinant gene expression within BL21*(DE3) E. coli cells, ion-exchange
chromatography on DEAE-Sephadex-A25 (medium), protein fractionation with ammonium sulfate and
gel filtration on Sephadex-G200. The developed method allows to obtain electrophoretically
homogeneous and functionally active Dps protein

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Published

2019-11-25

Issue

Vol. 12 No. 6 (2012): Sorbtsionnye i Khromatograficheskie Protsessy

Section

Статьи

How to Cite

Overexpression, isolation and purification of functionally active bacterioferritin Dps E.coli. (2019). Sorbtsionnye I Khromatograficheskie Protsessy, 12(6). https://journals.vsu.ru/sorpchrom/article/view/1891

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