Isoform expression in the multiple soluble malate dehydrogenase of Hoplias malabaricus (Erythrinidae, Characiformes)

Brazilian Journal of Biology

M. R. Aquino-silva²  M. L. B. Schwantes¹  A. R. Schwantes¹ 

[1] ,Universidade do Vale do Paraíba Faculdade de Engenharia e Arquitetura e Urbanismo São José dos Campos SP ,Brazil

关键词: isoforms;    sMDH;    Hoplias malabaricus;    recent locus duplication;    isoformas;    sMDH;    Hoplias malabaricus;    duplicação lócica recente;   

DOI  :  10.1590/S1519-69842003000100003

来源: SciELO

【 摘 要 】

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.

【 授权许可】

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