Purification and characterization of the flavoenzyme glutathione reductase from rat liver.

@article{Carlberg1975PurificationAC,
  title={Purification and characterization of the flavoenzyme glutathione reductase from rat liver.},
  author={Inger Carlberg and Bengt Mannervik},
  journal={The Journal of biological chemistry},
  year={1975},
  volume={250 14},
  pages={5475-80}
}
Glutathione reductase from rat liver has been purified greater than 5000-fold in a yield of 20%. The molecular weights of the enzyme and its subunits were estimated to be 125,000 and 60,000, respectively, indicating that the native enzyme is a dimer. The enzyme molecular contains 2 FAD molecules, which are reducible by NADPH, GSH or dithioerythritol. The reduced flavin is instantaneously reoxidized by addition of GSSG. The steady state kinetic data are consistent with a branching reaction… CONTINUE READING
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