Soluble malate dehydrogenase of Geophagus brasiliensis (Cichlidae, Perciformes): isolated isoforms and kinetics properties
Kinetic properties and thermal stabilities of Geophagus brasiliensis skeletal muscle unfractionated malate dehydrogenase (MDH, EC 1.1.1.37) and its isolated isoforms were analyzed to examine a possible sMDH-B* locus duplication in a fixation process influenced by genetic drift. Two optimal pHs were...
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Sociedade Brasileira de Genética
2008-01-01
|
| Series: | Genetics and Molecular Biology |
| Subjects: | |
| Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572008000200029 |
| _version_ | 1818320702474813440 |
|---|---|
| author | Maria Regina de Aquino-Silva Maria Luiza Barcellos Schwantes Flavia Simone Munin Arno Rudi Schwantes Silvana Pereira dos Santos |
| author_facet | Maria Regina de Aquino-Silva Maria Luiza Barcellos Schwantes Flavia Simone Munin Arno Rudi Schwantes Silvana Pereira dos Santos |
| author_sort | Maria Regina de Aquino-Silva |
| collection | DOAJ |
| description | Kinetic properties and thermal stabilities of Geophagus brasiliensis skeletal muscle unfractionated malate dehydrogenase (MDH, EC 1.1.1.37) and its isolated isoforms were analyzed to examine a possible sMDH-B* locus duplication in a fixation process influenced by genetic drift. Two optimal pHs were detected: 7.5 for AB1 unfractionated muscle phenotype and its B1 isoform, and 8.0 for AB1B2 unfractionated muscle phenotype, A and B2 isoforms. While G. brasiliensis A isoform could be characterized as thermostable, the duplicated B isoform cannot be assumed as thermolabile. Km values for isolated B2 isoforms were 1.6 times lower than for B1. A duplication event in progress best explains the electrophoretic six-band pattern detected in G. brasiliensis, which would be caused by genetic drift. |
| first_indexed | 2024-12-13T10:29:12Z |
| format | Article |
| id | doaj.art-43f5bf5240634f3d91bfc2c480b15be2 |
| institution | Directory Open Access Journal |
| issn | 1415-4757 1678-4685 |
| language | English |
| last_indexed | 2024-12-13T10:29:12Z |
| publishDate | 2008-01-01 |
| publisher | Sociedade Brasileira de Genética |
| record_format | Article |
| series | Genetics and Molecular Biology |
| spelling | doaj.art-43f5bf5240634f3d91bfc2c480b15be22022-12-21T23:50:56ZengSociedade Brasileira de GenéticaGenetics and Molecular Biology1415-47571678-46852008-01-0131133734210.1590/S1415-47572008000200029Soluble malate dehydrogenase of Geophagus brasiliensis (Cichlidae, Perciformes): isolated isoforms and kinetics propertiesMaria Regina de Aquino-SilvaMaria Luiza Barcellos SchwantesFlavia Simone MuninArno Rudi SchwantesSilvana Pereira dos SantosKinetic properties and thermal stabilities of Geophagus brasiliensis skeletal muscle unfractionated malate dehydrogenase (MDH, EC 1.1.1.37) and its isolated isoforms were analyzed to examine a possible sMDH-B* locus duplication in a fixation process influenced by genetic drift. Two optimal pHs were detected: 7.5 for AB1 unfractionated muscle phenotype and its B1 isoform, and 8.0 for AB1B2 unfractionated muscle phenotype, A and B2 isoforms. While G. brasiliensis A isoform could be characterized as thermostable, the duplicated B isoform cannot be assumed as thermolabile. Km values for isolated B2 isoforms were 1.6 times lower than for B1. A duplication event in progress best explains the electrophoretic six-band pattern detected in G. brasiliensis, which would be caused by genetic drift.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572008000200029gene duplicationsMDHsubstrate concentrationtemperaturepH isoforms |
| spellingShingle | Maria Regina de Aquino-Silva Maria Luiza Barcellos Schwantes Flavia Simone Munin Arno Rudi Schwantes Silvana Pereira dos Santos Soluble malate dehydrogenase of Geophagus brasiliensis (Cichlidae, Perciformes): isolated isoforms and kinetics properties Genetics and Molecular Biology gene duplication sMDH substrate concentration temperature pH isoforms |
| title | Soluble malate dehydrogenase of Geophagus brasiliensis (Cichlidae, Perciformes): isolated isoforms and kinetics properties |
| title_full | Soluble malate dehydrogenase of Geophagus brasiliensis (Cichlidae, Perciformes): isolated isoforms and kinetics properties |
| title_fullStr | Soluble malate dehydrogenase of Geophagus brasiliensis (Cichlidae, Perciformes): isolated isoforms and kinetics properties |
| title_full_unstemmed | Soluble malate dehydrogenase of Geophagus brasiliensis (Cichlidae, Perciformes): isolated isoforms and kinetics properties |
| title_short | Soluble malate dehydrogenase of Geophagus brasiliensis (Cichlidae, Perciformes): isolated isoforms and kinetics properties |
| title_sort | soluble malate dehydrogenase of geophagus brasiliensis cichlidae perciformes isolated isoforms and kinetics properties |
| topic | gene duplication sMDH substrate concentration temperature pH isoforms |
| url | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572008000200029 |
| work_keys_str_mv | AT mariareginadeaquinosilva solublemalatedehydrogenaseofgeophagusbrasiliensiscichlidaeperciformesisolatedisoformsandkineticsproperties AT marialuizabarcellosschwantes solublemalatedehydrogenaseofgeophagusbrasiliensiscichlidaeperciformesisolatedisoformsandkineticsproperties AT flaviasimonemunin solublemalatedehydrogenaseofgeophagusbrasiliensiscichlidaeperciformesisolatedisoformsandkineticsproperties AT arnorudischwantes solublemalatedehydrogenaseofgeophagusbrasiliensiscichlidaeperciformesisolatedisoformsandkineticsproperties AT silvanapereiradossantos solublemalatedehydrogenaseofgeophagusbrasiliensiscichlidaeperciformesisolatedisoformsandkineticsproperties |