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| Aquino-Silva,Maria Regina de; Schwantes,Maria Luiza Barcellos; Munin,Flavia Simone; Schwantes,Arno Rudi; Santos,Silvana Pereira dos. |
| 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... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Gene duplication; SMDH; Substrate concentration; Temperature; PH isoforms. |
| Ano: 2008 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572008000200029 |
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