Identification of S100b protein as copper-binding protein and its suppression of copper-induced cell damage.

@article{Nishikawa1997IdentificationOS,
  title={Identification of S100b protein as copper-binding protein and its suppression of copper-induced cell damage.},
  author={Toshio Nishikawa and Im Seon Lee and Naomasa Shiraishi and Takashi Ishikawa and Yoshihiro Ohta and Morimitsu Nishikimi},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 37},
  pages={23037-41}
}
We have isolated from bovine brain a protein with a high capacity to inhibit the copper ion-catalyzed oxidation of L-ascorbate and identified it as S100b protein, an EF-hand calcium-binding protein, by sequencing its proteolytic peptides. Copper binding studies showed that this protein has four copper-binding sites per dimeric protein molecule with a dissociation constant of 0.46 microM and that in the presence of L-ascorbate, copper ions bind to a total of six binding sites with a great… CONTINUE READING

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