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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)
Publication Information
Journal of Microbiology and Biotechnology / v.12, no.6, 2002 , pp. 986-988 More about this Journal
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
Shiga toxin; purification; heat treatment; overexpression;
Citations & Related Records
Times Cited By KSCI : 10  (Citation Analysis)
Times Cited By Web Of Science : 5  (Related Records In Web of Science)
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