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

نویسندگان

  • M R Aquino-Silva
  • M L Schwantes
  • A R Schwantes
چکیده

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.

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منابع مشابه

Hematological parameters of Hoplias malabaricus (Characiformes: Erythrinidae) parasitized by Monogenea in lagoons in Pirassununga, Brazil Parâmetros hematológicos de Hoplias malabaricus (Characiformes: Erythrinidae) parasitados por monogenea em lagoas de Pirassununga, Brasil

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عنوان ژورنال:
  • Brazilian journal of biology = Revista brasleira de biologia

دوره 63 1  شماره 

صفحات  -

تاریخ انتشار 2003