Isoform expression in the multiple soluble malate dehydrogenase of Hoplias malabaricus (Erythrinidae, Characiformes)
Braz. j. biol
;
63(1): 7-15, Feb. 2003. ilus, graf
Article
in English
| LILACS
| ID: lil-343407
RESUMO
Kinetic properties and thermal stabilities of Hoplias malabaricus liver and skeletal muscle unfractionated malate dehydrogenase (MDH, EC 1.1.1.37) and its isolated isoforms were analyzed to further study the possible sMDH-A* locus duplication evolved from a recent tandem duplication. Both A (A1 and A2) and B isoforms had similar optima pH (7.5-8.0). While Hoplias A isoform could not be characterized as thermostable, B could as thermolabile. A isoforms differed from B isoform in having higher Km values for oxaloacetate. The possibly duplicated A2 isoform showed higher substrate affinity than the A1. Hoplias duplicated A isoforms may influence the direction of carbon flow between glycolisis and gluconeogenesis
Full text:
Available
Index:
LILACS (Americas)
Main subject:
Gene Duplication
/
Fishes
/
Isoenzymes
/
Malate Dehydrogenase
Limits:
Animals
Language:
English
Journal:
Braz. j. biol
Journal subject:
Biology
Year:
2003
Type:
Article
Affiliation country:
Brazil
Institution/Affiliation country:
Universidade Federal de São Carlos/BR
/
Universidade do Vale do Paraíba/BR
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