Anti-oxidant enzymes in Cryptosporidium parvum oocysts.
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.
Entrala
E
E
Departmento Parasitologia, Facultad de Ciencias, Granada, Spain.
Mascaro
C
C
Barrett
J
J
D000818:Animals; D002374:Catalase / Q000032:analysis; D002417:Cattle; D003457:Cryptosporidiosis / Q000469:parasitology; D016785:Cryptosporidium parvum / Q000201:enzymology*; D005243:Feces / Q000469:parasitology; D005979:Glutathione Peroxidase / Q000032:analysis; D005980:Glutathione Reductase / Q000032:analysis; D005982:Glutathione Transferase / Q000032:analysis; D007526:Isoelectric Point; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000032:analysis; D010544:Peroxidases / Q000032:analysis; D013482:Superoxide Dismutase / Q000032:analysis* / Q000737:chemistry
D010544:Peroxidases; D002374:Catalase; D005979:Glutathione Peroxidase; D013482:Superoxide Dismutase; D009247:NADH, NADPH Oxidoreductases; C049608:trypanothione reductase; D005980:Glutathione Reductase; D005982:Glutathione Transferase