Purification and biochemical characterization of four iron superoxide dismutases in Trypanosoma cruzi

Detalhes bibliográficos
Autor(a) principal: Mateo,Héctor
Data de Publicação: 2008
Outros Autores: Marín,Clotilde, Pérez-Cordón,Gregorio, Sánchez-Moreno,Manuel
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Memórias do Instituto Oswaldo Cruz
Texto Completo: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762008000300008
Resumo: 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.
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spelling Purification and biochemical characterization of four iron superoxide dismutases in Trypanosoma cruzisuperoxide dismutaseT. cruzichromatographysubcellular localizationFour 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.Instituto Oswaldo Cruz, Ministério da Saúde2008-05-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762008000300008Memórias do Instituto Oswaldo Cruz v.103 n.3 2008reponame:Memórias do Instituto Oswaldo Cruzinstname:Fundação Oswaldo Cruzinstacron:FIOCRUZ10.1590/S0074-02762008000300008info:eu-repo/semantics/openAccessMateo,HéctorMarín,ClotildePérez-Cordón,GregorioSánchez-Moreno,Manueleng2020-04-25T17:50:17Zhttp://www.scielo.br/oai/scielo-oai.php0074-02761678-8060opendoar:null2020-04-26 02:15:34.395Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruztrue
dc.title.none.fl_str_mv Purification and biochemical characterization of four iron superoxide dismutases in Trypanosoma cruzi
title Purification and biochemical characterization of four iron superoxide dismutases in Trypanosoma cruzi
spellingShingle Purification and biochemical characterization of four iron superoxide dismutases in Trypanosoma cruzi
Mateo,Héctor
superoxide dismutase
T. cruzi
chromatography
subcellular localization
title_short Purification and biochemical characterization of four iron superoxide dismutases in Trypanosoma cruzi
title_full Purification and biochemical characterization of four iron superoxide dismutases in Trypanosoma cruzi
title_fullStr Purification and biochemical characterization of four iron superoxide dismutases in Trypanosoma cruzi
title_full_unstemmed Purification and biochemical characterization of four iron superoxide dismutases in Trypanosoma cruzi
title_sort Purification and biochemical characterization of four iron superoxide dismutases in Trypanosoma cruzi
author Mateo,Héctor
author_facet Mateo,Héctor
Marín,Clotilde
Pérez-Cordón,Gregorio
Sánchez-Moreno,Manuel
author_role author
author2 Marín,Clotilde
Pérez-Cordón,Gregorio
Sánchez-Moreno,Manuel
author2_role author
author
author
dc.contributor.author.fl_str_mv Mateo,Héctor
Marín,Clotilde
Pérez-Cordón,Gregorio
Sánchez-Moreno,Manuel
dc.subject.por.fl_str_mv superoxide dismutase
T. cruzi
chromatography
subcellular localization
topic superoxide dismutase
T. cruzi
chromatography
subcellular localization
dc.description.none.fl_txt_mv 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.
description 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.
publishDate 2008
dc.date.none.fl_str_mv 2008-05-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762008000300008
url http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762008000300008
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0074-02762008000300008
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Instituto Oswaldo Cruz, Ministério da Saúde
publisher.none.fl_str_mv Instituto Oswaldo Cruz, Ministério da Saúde
dc.source.none.fl_str_mv Memórias do Instituto Oswaldo Cruz v.103 n.3 2008
reponame:Memórias do Instituto Oswaldo Cruz
instname:Fundação Oswaldo Cruz
instacron:FIOCRUZ
reponame_str Memórias do Instituto Oswaldo Cruz
collection Memórias do Instituto Oswaldo Cruz
instname_str Fundação Oswaldo Cruz
instacron_str FIOCRUZ
institution FIOCRUZ
repository.name.fl_str_mv Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruz
repository.mail.fl_str_mv
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