Simple Purification of shiga Toxin B Chain from Recombinant Escherichia coli

  • Oh, Young-Phil (School of Food Science and Biotechnology, Woosong University) ;
  • Jeong, Seong-Tae (School of Food Science and Biotechnology, Woosong University) ;
  • Kim, Dae-Weon (School of Food Science and Biotechnology, Woosong University) ;
  • Kim, El-Chae (VaccTech Inc.) ;
  • Yoon, Ki-Hong (School of Food Science and Biotechnology, Woosong University)
  • Published : 2002.12.01

Abstract

A plasmid expression vector of pEStxl encoding a mature form of the B chain of the Shiga toxin was constructed without a signal peptide under the control of an inducible n promoter. The encoded protein was purified to 90% by simple heat treatment, and then further purified to 95% by Phenyl-Sepharose and DEAE-Sepharose chromatographies, all in a single day. Accordingly, this expression system and heat treatment could facilitate the rapid purification of gram-scale amounts of the Shiga toxin B subunit from recombinant Escherichia coli cells.

Keywords

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