Soluble malate dehydrogenase of Geophagus brasiliensis (Cichlidae, Perciformes): isolated isoforms and kinetics properties
Genet. mol. biol
;
31(1,suppl): 337-342, 2008. ilus, graf
Article
in English
| LILACS
| ID: lil-484608
ABSTRACT
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.
Full text:
Available
Index:
LILACS (Americas)
Main subject:
Perciformes
/
Malate Dehydrogenase
Limits:
Animals
Country/Region as subject:
South America
/
Brazil
Language:
English
Journal:
Genet. mol. biol
Journal subject:
Genetics
Year:
2008
Type:
Article
Affiliation country:
Brazil
Institution/Affiliation country:
Universidade Federal de São Carlos/BR
/
Universidade do Vale do Paraíba/BR
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