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Please use this identifier to cite or link to this item: http://hdl.handle.net/10481/32921

Title: Purification and biochemical characterization of four iron superoxide dismutases in Trypanosoma cruzi
Authors: Mateo Carrasco, Héctor
Marín Sánchez, Clotilde
Pérez-Cordón, Gregorio
Sánchez-Moreno, Manuel
Issue Date: 2008
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%, 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.
Sponsorship: Financial support: CGL2006-27889-E/BOS, Ministerio de Ciencia y Tecnología .
Publisher: Instituto Oswaldo Cruz
Keywords: Superoxide dismutase
Trypanosoma cruzi
Subcellular localization
URI: http://hdl.handle.net/10481/32921
ISSN: 0074-0276
Rights : Creative Commons Attribution-NonCommercial-NoDerivs 3.0 License
Citation: Mateo, H.; et al. Purification and biochemical characterization of four iron superoxide dismutases in Trypanosoma cruzi. Memorias do Instituto Oswaldo Cruz, 103(3): 271-276 (2008). [http://hdl.handle.net/10481/32921]
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