Genetics and Molecular Biology | |
Soluble malate dehydrogenase of Geophagus brasiliensis (Cichlidae, Perciformes): isolated isoforms and kinetics properties | |
Maria Regina De Aquino-silva2  Maria Luiza Barcellos Schwantes1  Flavia Simone Munin1  Arno Rudi Schwantes1  Silvana Pereira Dos Santos2  | |
[1] ,Universidade do Vale do Paraíba Instituto de Pesquisa & Desenvolvimento São José dos Campos SP ,Brazil | |
关键词: gene duplication; sMDH; substrate concentration; temperature; pH isoforms; | |
DOI : 10.1590/S1415-47572008000200029 | |
来源: SciELO | |
【 摘 要 】
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.
【 授权许可】
CC BY
All the contents of this journal, except where otherwise noted, is licensed under a Creative Commons Attribution License
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