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Superoxide radical dismutation by copper proteins

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Abstract

The catalytic effects of human superoxide dismutase and bovine ceruloplasmin on superoxide radical dismutation were studied by pulse radiolysis at room temperature. The rate constants for the disappearance of superoxide radicals were found to be (8.1±1.2)·105M−1·s−1 for spontaneous disproportionation, (9.8±1.5)·106 M−1·s−1 in the presence of ceruloplasmin, and (2.1±0.3)·109M−1·s−1 in the presence of superoxide dismutase.

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Authors and Affiliations

  1. Institute of Applied Radiation Chemistry, Technical University of łódź, 93-590, łódź, (Poland)

    A. Plonka, J. Mayer, D. Metodiewa & J. L. Gebicki

  2. Institute of Biochemistry and Biophysics, University of Łódź, 90-237, Łódź, (Poland)

    A. Zgirski & M. Grabska

Authors
  1. A. Plonka
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  2. J. Mayer
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  3. D. Metodiewa
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  4. J. L. Gebicki
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  5. A. Zgirski
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  6. M. Grabska
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Plonka, A., Mayer, J., Metodiewa, D. et al. Superoxide radical dismutation by copper proteins. Journal of Radioanalytical and Nuclear Chemistry, Articles 101, 221–225 (1986). https://doi.org/10.1007/BF02042422

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  • DOI: https://doi.org/10.1007/BF02042422

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