Modification of cysteine 111 in human Cu,Zn-superoxide dismutase.

@article{OkadoMatsumoto2006ModificationOC,
  title={Modification of cysteine 111 in human Cu,Zn-superoxide dismutase.},
  author={Ayako Okado-Matsumoto and Ziqiang Guan and Irwin Fridovich},
  journal={Free radical biology & medicine},
  year={2006},
  volume={41 12},
  pages={1837-46}
}
Human Cu,Zn-superoxide dismutase (hSOD1) has 4 cysteines per subunit. Cys57 and Cys148 are involved in an intrasubunit disulfide bond, while Cys6 and Cys111 are free. Cys6 is buried within the protein while Cys111 is on the surface, near the dimer interface. We examined by liquid chromatography-mass spectrometry the commercially purchased hSOD1 isolated from erythrocytes as well as hSOD1s isolated from human erythrocytes, brain, and hSOD1 expressed in Sf9, yeast, and E. coli. Our goal was to… CONTINUE READING

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