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 COENZYME Q10 400 MG 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 lotion 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.