Soluble malate dehydrogenase of Geophagus brasiliensis (Cichlidae, Perciformes): isolated isoforms and kinetics properties
In: Genetics and Molecular Biology, Jg. 31 (2008), Heft 1
Online
academicJournal
Zugriff:
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.
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Soluble malate dehydrogenase of Geophagus brasiliensis (Cichlidae, Perciformes): isolated isoforms and kinetics properties
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Autor/in / Beteiligte Person: | Aquino-Silva, Maria Regina de ; Schwantes, Maria Luiza Barcellos ; Munin, Flavia Simone ; Schwantes, Arno Rudi ; Santos, Silvana Pereira dos |
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Zeitschrift: | Genetics and Molecular Biology, Jg. 31 (2008), Heft 1 |
Veröffentlichung: | Sociedade Brasileira de Genética, 2008 |
Medientyp: | academicJournal |
ISSN: | 1415-4757 (print) |
DOI: | 10.1590/S1415-47572008000200029 |
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