Characterization of the role of protein–cysteine residues in the binding with sodium arsenite

@article{Chang2012CharacterizationOT,
  title={Characterization of the role of protein–cysteine residues in the binding with sodium arsenite},
  author={Yu-ying Chang and T. Kuo and Chun-Hua Hsu and D. Hou and Y. Kao and Rong-Nan Huang},
  journal={Archives of Toxicology},
  year={2012},
  volume={86},
  pages={911-922}
}
To better characterize the interaction of protein–cysteines with sodium arsenite, arsenic-binding proteins were identified from the arsenic-resistant Chinese hamster ovary cell line SA7 using a p-aminophenylarsine oxide (PAO)-agarose matrix in combination with proteomic techniques. Twenty of the isolated arsenic-binding proteins were further peptide-mapped by MALDI-Q-TOF-MS. The binding capacity of PAO-agarose-retained proteins was then verified by re-applying Escherichia coli overexpressed… Expand
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