A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity.

@article{Tamura1996ANS,
  title={A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity.},
  author={Takashi Tamura and Thressa Campbell Stadtman},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1996},
  volume={93 3},
  pages={
          1006-11
        }
}
  • T. TamuraT. Stadtman
  • Published 6 February 1996
  • Biology, Chemistry
  • Proceedings of the National Academy of Sciences of the United States of America
We report the isolation and characterization of a new selenoprotein from a human lung adenocarcinoma cell line, NCI-H441. Cells were grown in RPMI-1640 medium containing 10% (vol/vol) fetal bovine serum and 0.1 microM [75Se]selenite. A 75Se-labeled protein was isolated from sonic extracts of the cells by chromatography on DE-23, phenyl-Sepharose, heparin-agarose, and butyl-Sepharose. The protein, a homodimer of 57-kDa subunits, was shown to contain selenium in the form of selenocysteine… 
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39 References

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A small, heat-stable selenoprotein, one of the components of the glycine reductase complex, was labeled with 75Se by growth of Clostridium sticklandii in the presence of Na2 75SeO3 and the selenium-containing moiety was shown to be a selenocysteine residue.

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