Purification, characterization, and glutathione binding to selenoprotein W from monkey muscle.

@article{Gu1999PurificationCA,
  title={Purification, characterization, and glutathione binding to selenoprotein W from monkey muscle.},
  author={Q. P. Gu and Michael A. Beilstein and Elizabeth Barofsky and Walt Ream and Phil D. Whanger},
  journal={Archives of biochemistry and biophysics},
  year={1999},
  volume={361 1},
  pages={25-33}
}
Selenoprotein W was purified from monkey skeletal muscle to investigate its binding of glutathione. The purification was accomplished by concentration of the cytosol with an Amicon cell, gel filtration using Sephadex G-50, cation-exchange chromatography with CM-Sephadex, and reverse-phase high-pressure liquid chromatography using a C-18 Vydac column. Selenoprotein W was monitored during purification by slot blots. These steps resulted in an electrophoretically pure selenoprotein W preparation… CONTINUE READING

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