Highly active dimeric and low-activity tetrameric forms of selenium-containing rat thioredoxin reductase 1.

@article{Rengby2009HighlyAD,
  title={Highly active dimeric and low-activity tetrameric forms of selenium-containing rat thioredoxin reductase 1.},
  author={Olle Rengby and Qing Cheng and Marie Vahter and Hans J{\"o}rnvall and Elias S. J. Arn{\'e}r},
  journal={Free radical biology & medicine},
  year={2009},
  volume={46 7},
  pages={893-904}
}
Mammalian thioredoxin reductase 1 (TrxR1) is a selenoprotein that contains a selenocysteine (Sec) residue at the penultimate C-terminal position. When rat TrxR1 is expressed recombinantly in Escherichia coli, partial truncation at the Sec-encoding UGA gives rise to additional protein species that lack Sec. Phenylarsine oxide (PAO) Sepharose can subsequently be used to enrich the Sec-containing protein and yield activity corresponding to that of native enzyme. Herein we extensively purified… CONTINUE READING
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