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Reactions of Myeloperoxidase with Superoxide and Hydrogen Peroxide: Signficance for its Function in the Neutrophil

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Oxygen Radicals in Biology and Medicine

Part of the book series: Basic Life Sciences ((BLSC,volume 49))

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Abstract

Myeloperoxidase (MPO) in its purified form acts as a conventional peroxidase and, in addition, catalyses the reaction

It has a pH optimum of 5–6, but shows some activity at neutral pH. HOCl and the MPO-H2O2-Cl- system are very reactive with most biological molecules, and both are potently microbicidal. Thus the MPO system seems the ideal candidate to provide the neutrophil with antimicrobial activity.

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References

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Author information

Authors and Affiliations

  1. Pathology Department, Christchurch School of Medicine, Christchurch, New Zealand

    Christine C. Winterbourn & Anthony J. Kettle

Authors
  1. Christine C. Winterbourn
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  2. Anthony J. Kettle
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Editor information

Editors and Affiliations

  1. National Bureau of Standards, Gaithersburg, Maryland, USA

    Michael G. Simic

  2. International Life Sciences Institute, Washington, D.C., USA

    Karen A. Taylor

  3. Univesity of California, San Diego, La Jolla, California, USA

    John F. Ward

  4. Max-Planck-Institut für Strahlenchemie, Mülheim a.d. Ruhr, Federal Republic of Germany

    Clemens von Sonntag

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© 1988 Plenum Press, New York

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Winterbourn, C.C., Kettle, A.J. (1988). Reactions of Myeloperoxidase with Superoxide and Hydrogen Peroxide: Signficance for its Function in the Neutrophil. In: Simic, M.G., Taylor, K.A., Ward, J.F., von Sonntag, C. (eds) Oxygen Radicals in Biology and Medicine. Basic Life Sciences, vol 49. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5568-7_132

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  • DOI: https://doi.org/10.1007/978-1-4684-5568-7_132

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-5570-0

  • Online ISBN: 978-1-4684-5568-7

  • eBook Packages: Springer Book Archive

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