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Anti-oxidant enzymes in Cryptosporidium parvum oocysts

Published online by Cambridge University Press:  01 January 1997

E. ENTRALA ,
C. MASCARO  and
J. BARRETT
E. ENTRALA
Affiliation:
Departmento Parasitologia, Facultad de Ciencias, Campus Fuentenueva, E-18071 Granada, Spain
C. MASCARO
Affiliation:
Departmento Parasitologia, Facultad de Ciencias, Campus Fuentenueva, E-18071 Granada, Spain
J. BARRETT
Affiliation:
Institute of Biological Sciences, University of Wales, Aberystwyth, Dyfed SY23 3DA
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Abstract

Oocysts of Cryptosporidium parvum showed relatively low levels of SOD activity. The SOD which had a pI of 4.8 and an approximate molecular weight of 35 kDa appeared to be iron dependent. Catalase, glutathione transferase, glutathione reductase and glutathione peroxidase activity could not be detected, nor could trypanothione reductase. No NADH or NADPH oxidase activity could be detected, nor could peroxidase activity be demonstrated using o-dianisidine, guaiacol, NADPH or NADH as co-substrates. However, an NADPH-dependent H2O2 scavenging system was detected in the insoluble fraction.

Keywords

Cryptosporidium parvumanti-oxidant enzymesSOD
Type
Research Article
Information
Parasitology , Volume 114 , Issue 1 , January 1997 , pp. 13 - 17
Copyright
© 1997 Cambridge University Press

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