Efficient solubilization, activation, and purification of recombinant Cry45Aa of Bacillus thuringiensis expressed as inclusion bodies in Escherichia coli.

@article{Okumura2006EfficientSA,
  title={Efficient solubilization, activation, and purification of recombinant Cry45Aa of Bacillus thuringiensis expressed as inclusion bodies in Escherichia coli.},
  author={Shiro Okumura and Hiroyuki Saitoh and Naoya Wasano and Hideki Katayama and Kazuhiko Higuchi and Eiichi Mizuki and Kuniyo Inouye},
  journal={Protein expression and purification},
  year={2006},
  volume={47 1},
  pages={144-51}
}
A cytotoxic protein Cry45Aa of Bacillus thuringiensis expressed as inclusion bodies in Escherichia coli was solubilized in 10 mM HCl. Protein concentration of saturated solution of the recombinant Cry45Aa in 10 mM HCl was about 25 times higher than that in the buffer of previous method (in 50 mM sodium carbonate buffer, pH 10.5, containing 1 mM EDTA, and 10 mM dithiothreitol). The Cry45Aa solubilized in the acidic solution was activated by pepsin as an alternative to proteinase K in the… CONTINUE READING

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