The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase.

@article{Bjrnstedt1994TheTA,
  title={The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase.},
  author={Mikael Bj{\"o}rnstedt and Jia-dan Xue and Wenya Huang and Bj{\"o}rn {\AA}kesson and Anders Holmgren},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 47},
  pages={
          29382-4
        }
}
Human plasma glutathione peroxidase (GSH-Px) is a distinct extracellular selenoenzyme that detoxifies hydroperoxides when used with GSH in high (mM) non-physiological concentrations. We have discovered that NADPH and human thioredoxin reductase (TR) by itself or with thioredoxin (Trx) are efficient electron donors to this human plasma peroxidase. Incubation of 0.05 microM TR with 0.25 microM GSH-Px, in a system free from GSH, resulted in reduction of t-butyl hydroperoxide. Addition of Trx, 2.5… CONTINUE READING

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