Purification and biochemical characterization of four iron superoxide dismutases in Trypanosoma cruzi
Mem. Inst. Oswaldo Cruz
;
103(3): 271-276, May 2008. ilus, graf, tab
Artículo
en Inglés
| LILACS
| ID: lil-485219
ABSTRACT
Four superoxide dismutase (SOD) activities (SOD I, II, III, and IV) have been characterized in the epimastigote form of Trypanosoma cruzi. The total extract was subjected to two successive ammonium sulphate additions between 35 and 85 percent, and the resulting fraction was purified using two continuous chromatography processes (ion exchange and filtration). Enzymes were insensitive to cyanide but sensitive to hydrogen peroxide, properties characteristic of iron-containing SODs. The molecular masses of the different SODs were 20 kDa (SOD I), 60 kDa (SOD II), 50 kDa (SOD III) and 25 kDa (SOD IV), whereas the isoelectric points were 6.9, 6.8, 5.2 and 3.8, respectively. Subcellular location and digitonin experiments have shown that these SODs are mainly cytosolic, with small amounts in the low-mass organelles (SOD II and SOD I) and the mitochondrion (SOD III), where these enzymes play an important role in minimizing oxidative damage.
Texto completo:
Disponible
Índice:
LILACS (Américas)
Asunto principal:
Superóxido Dismutasa
/
Trypanosoma cruzi
Límite:
Animales
Idioma:
Inglés
Revista:
Mem. Inst. Oswaldo Cruz
Asunto de la revista:
Medicina Tropical
/
Parasitología
Año:
2008
Tipo del documento:
Artículo
/
Documento de proyecto
País de afiliación:
España
Institución/País de afiliación:
Universidad de Granada/ES
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