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Endogenous superoxide dismutase activity in two Babesia species

Published online by Cambridge University Press:  06 April 2009

P. Becuwe ,
C. Slomianny ,
A. Valentin ,
J. Schrevel ,
D. Camus  and
D. Dive
P. Becuwe
Affiliation:
INSERM U42, B.P.39, 59651 Villeneuve d'Ascq cedex, France
C. Slomianny
Affiliation:
INSERM U42, B.P.39, 59651 Villeneuve d'Ascq cedex, France
A. Valentin
Affiliation:
Laboratoire de Biologie Cellulaire, URA CNRS 290, 40 Avenue du Recteur Pineau, 86022 Poitiers, France
J. Schrevel
Affiliation:
Laboratoire de Biologie Cellulaire, URA CNRS 290, 40 Avenue du Recteur Pineau, 86022 Poitiers, France Laboratoire de Biologie Parasitaire et Chimiothérapie, Muséum National d'Histoire Naturelle, 61 rue Buffon, 75231 Paris cedex 05, France
D. Camus
Affiliation:
Laboratoire de Biologie Cellulaire, URA CNRS 290, 40 Avenue du Recteur Pineau, 86022 Poitiers, France
D. Dive
Affiliation:
Laboratoire de Biologie Cellulaire, URA CNRS 290, 40 Avenue du Recteur Pineau, 86022 Poitiers, France
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Summary

Babesia hylomysci and B. divergens were studied for superoxide dismutase (SOD) activity by enzyme assay and isoelectric focusing (IEF). In the two Babesia species, parasite-associated SOD is cyanide-insensitive and inhibited by H2 O2, indicating that iron is the cofactor metal. Measurements of SOD activity from purified parasites show that the SOD activity detected in Babesia is, for the main part, due to an endogenous enzyme.

Keywords

Babesiasuperoxide dismutaseiron
Type
Research Article
Information
Parasitology , Volume 105 , Issue 2 , October 1992 , pp. 177 - 182
Copyright
Copyright © Cambridge University Press 1992

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References

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