Role of the Dimeric Structure in Cu,Zn Superoxide Dismutase

@article{Battistoni1998RoleOT,
  title={Role of the Dimeric Structure in Cu,Zn Superoxide Dismutase},
  author={A. Battistoni and S. Folcarelli and L. Cervoni and F. Polizio and A. Desideri and A. Giartosio and G. Rotilio},
  journal={The Journal of Biological Chemistry},
  year={1998},
  volume={273},
  pages={5655 - 5661}
}
  • A. Battistoni, S. Folcarelli, +4 authors G. Rotilio
  • Published 1998
  • Medicine, Chemistry
  • The Journal of Biological Chemistry
  • To investigate the structural/functional role of the dimeric structure in Cu,Zn superoxide dismutases, we have studied the stability to a variety of agents of the Escherichia coli enzyme, the only monomeric variant of this class so far isolated. Differential scanning calorimetry of the native enzyme showed the presence of two well defined peaks identified as the metal free and holoprotein. Unlike dimeric Cu,Zn superoxide dismutases, the unfolding of the monomeric enzyme was found to be highly… CONTINUE READING

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