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
em En
| LILACS
| ID: lil-343407
Biblioteca responsável:
BR1.1
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
Texto completo:
1
Coleções:
01-internacional
Base de dados:
LILACS
Assunto principal:
Duplicação Gênica
/
Peixes
/
Isoenzimas
/
Malato Desidrogenase
Limite:
Animals
Idioma:
En
Revista:
Braz. j. biol
Assunto da revista:
BIOLOGIA
Ano de publicação:
2003
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Brasil