Purification and biochemical characterization of an organic-solvent-tolerant thioredoxin from dromedary pancreas.

@article{Bacha2012PurificationAB,
  title={Purification and biochemical characterization of an organic-solvent-tolerant thioredoxin from dromedary pancreas.},
  author={Abir G Ben Bacha and Hafedh Mejdoub},
  journal={The protein journal},
  year={2012},
  volume={31 1},
  pages={1-7}
}
We purified to homogeneity and characterized a heat stable thioredoxin which catalyzes thiol/disulfide exchange reaction, for the first time from dromedary pancreas. The purification involved heat and acidic treatment (90 °C; pH 2.5), precipitation by ammonium sulphate and ethanol, respectively followed by sequential column chromatography reverse HPLC column, and it resulted in an apparently pure protein after a 217-fold purification with a final yield of 55% of the initial thioredoxin activity… CONTINUE READING

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Mammal Genome 18:197–209

M Yu, B Geiger, N Deeb, MF Rothschild
2007
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