Isoform expression in the multiple soluble malate dehydrogenase of Hoplias malabaricus (Erythrinidae, Characiformes)

Detalhes bibliográficos
Autor(a) principal: Aquino-Silva,M. R.
Data de Publicação: 2003
Outros Autores: Schwantes,M. L. B., Schwantes,A. R.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Journal of Biology
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842003000100003
Resumo: Kinetic properties and thermal stabilities of Hoplias malabaricus liver and skeletal muscle unfractionated malate dehydrogenase (MDH, EC 1.1.1.37) and its isolated isoforms were analyzed to further study the possible sMDH-A* locus duplication evolved from a recent tandem duplication. Both A (A1 and A2) and B isoforms had similar optima pH (7.5-8.0). While Hoplias A isoform could not be characterized as thermostable, B could as thermolabile. A isoforms differed from B isoform in having higher Km values for oxaloacetate. The possibly duplicated A2 isoform showed higher substrate affinity than the A1. Hoplias duplicated A isoforms may influence the direction of carbon flow between glycolisis and gluconeogenesis.
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spelling Isoform expression in the multiple soluble malate dehydrogenase of Hoplias malabaricus (Erythrinidae, Characiformes)isoformssMDHHoplias malabaricusrecent locus duplicationKinetic properties and thermal stabilities of Hoplias malabaricus liver and skeletal muscle unfractionated malate dehydrogenase (MDH, EC 1.1.1.37) and its isolated isoforms were analyzed to further study the possible sMDH-A* locus duplication evolved from a recent tandem duplication. Both A (A1 and A2) and B isoforms had similar optima pH (7.5-8.0). While Hoplias A isoform could not be characterized as thermostable, B could as thermolabile. A isoforms differed from B isoform in having higher Km values for oxaloacetate. The possibly duplicated A2 isoform showed higher substrate affinity than the A1. Hoplias duplicated A isoforms may influence the direction of carbon flow between glycolisis and gluconeogenesis.Instituto Internacional de Ecologia2003-02-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842003000100003Brazilian Journal of Biology v.63 n.1 2003reponame:Brazilian Journal of Biologyinstname:Instituto Internacional de Ecologia (IIE)instacron:IIE10.1590/S1519-69842003000100003info:eu-repo/semantics/openAccessAquino-Silva,M. R.Schwantes,M. L. B.Schwantes,A. R.eng2003-08-14T00:00:00Zoai:scielo:S1519-69842003000100003Revistahttps://www.scielo.br/j/bjb/https://old.scielo.br/oai/scielo-oai.phpbjb@bjb.com.br||bjb@bjb.com.br1678-43751519-6984opendoar:2003-08-14T00:00Brazilian Journal of Biology - Instituto Internacional de Ecologia (IIE)false
dc.title.none.fl_str_mv Isoform expression in the multiple soluble malate dehydrogenase of Hoplias malabaricus (Erythrinidae, Characiformes)
title Isoform expression in the multiple soluble malate dehydrogenase of Hoplias malabaricus (Erythrinidae, Characiformes)
spellingShingle Isoform expression in the multiple soluble malate dehydrogenase of Hoplias malabaricus (Erythrinidae, Characiformes)
Aquino-Silva,M. R.
isoforms
sMDH
Hoplias malabaricus
recent locus duplication
title_short Isoform expression in the multiple soluble malate dehydrogenase of Hoplias malabaricus (Erythrinidae, Characiformes)
title_full Isoform expression in the multiple soluble malate dehydrogenase of Hoplias malabaricus (Erythrinidae, Characiformes)
title_fullStr Isoform expression in the multiple soluble malate dehydrogenase of Hoplias malabaricus (Erythrinidae, Characiformes)
title_full_unstemmed Isoform expression in the multiple soluble malate dehydrogenase of Hoplias malabaricus (Erythrinidae, Characiformes)
title_sort Isoform expression in the multiple soluble malate dehydrogenase of Hoplias malabaricus (Erythrinidae, Characiformes)
author Aquino-Silva,M. R.
author_facet Aquino-Silva,M. R.
Schwantes,M. L. B.
Schwantes,A. R.
author_role author
author2 Schwantes,M. L. B.
Schwantes,A. R.
author2_role author
author
dc.contributor.author.fl_str_mv Aquino-Silva,M. R.
Schwantes,M. L. B.
Schwantes,A. R.
dc.subject.por.fl_str_mv isoforms
sMDH
Hoplias malabaricus
recent locus duplication
topic isoforms
sMDH
Hoplias malabaricus
recent locus duplication
description Kinetic properties and thermal stabilities of Hoplias malabaricus liver and skeletal muscle unfractionated malate dehydrogenase (MDH, EC 1.1.1.37) and its isolated isoforms were analyzed to further study the possible sMDH-A* locus duplication evolved from a recent tandem duplication. Both A (A1 and A2) and B isoforms had similar optima pH (7.5-8.0). While Hoplias A isoform could not be characterized as thermostable, B could as thermolabile. A isoforms differed from B isoform in having higher Km values for oxaloacetate. The possibly duplicated A2 isoform showed higher substrate affinity than the A1. Hoplias duplicated A isoforms may influence the direction of carbon flow between glycolisis and gluconeogenesis.
publishDate 2003
dc.date.none.fl_str_mv 2003-02-01
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://old.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842003000100003
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842003000100003
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1519-69842003000100003
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 Internacional de Ecologia
publisher.none.fl_str_mv Instituto Internacional de Ecologia
dc.source.none.fl_str_mv Brazilian Journal of Biology v.63 n.1 2003
reponame:Brazilian Journal of Biology
instname:Instituto Internacional de Ecologia (IIE)
instacron:IIE
instname_str Instituto Internacional de Ecologia (IIE)
instacron_str IIE
institution IIE
reponame_str Brazilian Journal of Biology
collection Brazilian Journal of Biology
repository.name.fl_str_mv Brazilian Journal of Biology - Instituto Internacional de Ecologia (IIE)
repository.mail.fl_str_mv bjb@bjb.com.br||bjb@bjb.com.br
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