Tetrameric and dimeric malate dehydrogenase isoenzymes in Trypanosoma cruzi epimastigotes

Two malate dehydrogenase isoforms, named MDH1 and MDH2, have been purified to homogeneity from Trypanosoma cruzi epimastigotes. Both enzymes consist of subunits with a molecular mass close to 33 kDa; native molecular mass determination by gel filtration, however, indicated that MDH1 is a dimer, wher...

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Detalhes bibliográficos
Autores: Reynoso Hunter, Giselle, Hellman, Ulf, Cazzulo, Juan Jose, Nowicki, Cristina
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2000
País:Argentina
Recursos:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/39152
Acesso em linha:http://hdl.handle.net/11336/39152
Access Level:acceso abierto
Palavra-chave:Mdh1
Mdh2
Trypanosoma Cruzi
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
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spelling Tetrameric and dimeric malate dehydrogenase isoenzymes in Trypanosoma cruzi epimastigotesReynoso Hunter, GiselleHellman, UlfCazzulo, Juan JoseNowicki, CristinaMdh1Mdh2Trypanosoma Cruzihttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Two malate dehydrogenase isoforms, named MDH1 and MDH2, have been purified to homogeneity from Trypanosoma cruzi epimastigotes. Both enzymes consist of subunits with a molecular mass close to 33 kDa; native molecular mass determination by gel filtration, however, indicated that MDH1 is a dimer, whereas MDH2 is a tetramer. Both isoforms did not cross-react immunologically. The N-termini of both MDH isoforms and several tryptic peptides of MDH1 (amounting to about one third of the complete molecule) have been sequenced by automated Edman degradation. The tryptic digests of both enzymes have also been analysed by mass spectrometry (MALDI-TOF MS). The apparent K(m) values in both directions of the reaction have been determined, as well as the possible inhibition by excess of the substrate oxaloacetate. The sequence data, together with the pI values and the presence or absence of oxaloacetate inhibition indicate that the dimeric MDH1 is the mitochondrial isoenzyme, whereas the tetrameric MDH2 is the glycosomal isoenzyme. No evidence was found for the presence of a cytosolic isoform. (C) 2000 Elsevier Science B.V.Fil: Reynoso Hunter, Giselle. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Hellman, Ulf. Ludwig Institute for Cancer Research; SueciaFil: Cazzulo, Juan Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; ArgentinaFil: Nowicki, Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaElsevier Science2000-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/39152Reynoso Hunter, Giselle; Hellman, Ulf; Cazzulo, Juan Jose; Nowicki, Cristina; Tetrameric and dimeric malate dehydrogenase isoenzymes in Trypanosoma cruzi epimastigotes; Elsevier Science; Molecular and Biochemical Parasitology; 105; 2; 2-2000; 203-2140166-6851CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0166685199001760info:eu-repo/semantics/altIdentifier/doi/10.1016/S0166-6851(99)00176-0info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2024-05-08T13:41:04Zoai:ri.conicet.gov.ar:11336/39152instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982024-05-08 13:41:04.21CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Tetrameric and dimeric malate dehydrogenase isoenzymes in Trypanosoma cruzi epimastigotes
title Tetrameric and dimeric malate dehydrogenase isoenzymes in Trypanosoma cruzi epimastigotes
spellingShingle Tetrameric and dimeric malate dehydrogenase isoenzymes in Trypanosoma cruzi epimastigotes
Reynoso Hunter, Giselle
Mdh1
Mdh2
Trypanosoma Cruzi
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
title_short Tetrameric and dimeric malate dehydrogenase isoenzymes in Trypanosoma cruzi epimastigotes
title_full Tetrameric and dimeric malate dehydrogenase isoenzymes in Trypanosoma cruzi epimastigotes
title_fullStr Tetrameric and dimeric malate dehydrogenase isoenzymes in Trypanosoma cruzi epimastigotes
title_full_unstemmed Tetrameric and dimeric malate dehydrogenase isoenzymes in Trypanosoma cruzi epimastigotes
title_sort Tetrameric and dimeric malate dehydrogenase isoenzymes in Trypanosoma cruzi epimastigotes
dc.creator.none.fl_str_mv Reynoso Hunter, Giselle
Hellman, Ulf
Cazzulo, Juan Jose
Nowicki, Cristina
author Reynoso Hunter, Giselle
author_facet Reynoso Hunter, Giselle
Hellman, Ulf
Cazzulo, Juan Jose
Nowicki, Cristina
author_role author
author2 Hellman, Ulf
Cazzulo, Juan Jose
Nowicki, Cristina
author2_role author
author
author
dc.subject.none.fl_str_mv Mdh1
Mdh2
Trypanosoma Cruzi
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
topic Mdh1
Mdh2
Trypanosoma Cruzi
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
description Two malate dehydrogenase isoforms, named MDH1 and MDH2, have been purified to homogeneity from Trypanosoma cruzi epimastigotes. Both enzymes consist of subunits with a molecular mass close to 33 kDa; native molecular mass determination by gel filtration, however, indicated that MDH1 is a dimer, whereas MDH2 is a tetramer. Both isoforms did not cross-react immunologically. The N-termini of both MDH isoforms and several tryptic peptides of MDH1 (amounting to about one third of the complete molecule) have been sequenced by automated Edman degradation. The tryptic digests of both enzymes have also been analysed by mass spectrometry (MALDI-TOF MS). The apparent K(m) values in both directions of the reaction have been determined, as well as the possible inhibition by excess of the substrate oxaloacetate. The sequence data, together with the pI values and the presence or absence of oxaloacetate inhibition indicate that the dimeric MDH1 is the mitochondrial isoenzyme, whereas the tetrameric MDH2 is the glycosomal isoenzyme. No evidence was found for the presence of a cytosolic isoform. (C) 2000 Elsevier Science B.V.
publishDate 2000
dc.date.none.fl_str_mv 2000-02
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/39152
Reynoso Hunter, Giselle; Hellman, Ulf; Cazzulo, Juan Jose; Nowicki, Cristina; Tetrameric and dimeric malate dehydrogenase isoenzymes in Trypanosoma cruzi epimastigotes; Elsevier Science; Molecular and Biochemical Parasitology; 105; 2; 2-2000; 203-214
0166-6851
CONICET Digital
CONICET
url http://hdl.handle.net/11336/39152
identifier_str_mv Reynoso Hunter, Giselle; Hellman, Ulf; Cazzulo, Juan Jose; Nowicki, Cristina; Tetrameric and dimeric malate dehydrogenase isoenzymes in Trypanosoma cruzi epimastigotes; Elsevier Science; Molecular and Biochemical Parasitology; 105; 2; 2-2000; 203-214
0166-6851
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0166685199001760
info:eu-repo/semantics/altIdentifier/doi/10.1016/S0166-6851(99)00176-0
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 15,228081

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