Purification and biochemical characterization of four iron superoxide dismutases in Trypanosoma cruzi Mateo Carrasco, Héctor Marín Sánchez, Clotilde Pérez-Cordón, Gregorio Sánchez Moreno, Manuel Superoxide dismutase Trypanosoma cruzi Chromatography Subcellular localization 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. 2014-09-05T12:19:17Z 2014-09-05T12:19:17Z 2008 journal article 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] 0074-0276 http://hdl.handle.net/10481/32921 10.1590/S0074-02762008000300008 eng http://creativecommons.org/licenses/by-nc-nd/3.0/ open access Creative Commons Attribution-NonCommercial-NoDerivs 3.0 License Instituto Oswaldo Cruz