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Brazilian Journal of Biology

Print version ISSN 1519-6984On-line version ISSN 1678-4375

Abstract

AQUINO-SILVA, M. R.; SCHWANTES, M. L. B.  and  SCHWANTES, A. R.. Isoform expression in the multiple soluble malate dehydrogenase of Hoplias malabaricus (Erythrinidae, Characiformes). Braz. J. Biol. [online]. 2003, vol.63, n.1, pp.7-15. ISSN 1519-6984.  http://dx.doi.org/10.1590/S1519-69842003000100003.

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.

Keywords : isoforms; sMDH; Hoplias malabaricus; recent locus duplication.

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