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 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.
| Main Authors: | , , , , |
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| Format: | Digital revista |
| Language: | English |
| Published: |
Sociedade Brasileira de Genética
2008
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| Online Access: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572008000200029 |
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