Description_x000D_ General description_x000D_ Malic Dehydrogenase is a ubiquitous enzyme, which exists in two isoforms in eukaryotic cells._x000D_ Malic dehydrogenase exists as a dimer with each subunit containing an NAD-binding domain and a substrate-binding carboxy-terminal domain required for activity._x000D_ Application_x000D_ Malic Dehydrogenase from porcine heart has been used:_x000D_ • in qualitative protein binding measurements_x000D_ • to test internally calibrated electrochemical continuous enzyme assay (ICECEA) with model enzyme pair_x000D_ • to investigate the effect of chaperone on the refolding of heat-denatured malate dehydrogenase_x000D_ Malic dehydrogenase has been used in a study to assess the effect of an immunomodulator S2 complex on the enzymes of the parasites. It has also been used in a study to investigate the heterogeneity of lactic and malic dehydrogenase in cerebrospinal fluid._x000D_ Biochem/physiol Actions_x000D_ Malic Dehydrogenase (MDH) plays an important role in the citric acid cycle in mitochondria. It catalyzes the interconversion of substrates malate and oxaloacetate with the simultaneous oxidation/reduction of NAD/NADH+. MDH present in the cytosol is involved in the shuttling of malate/aspartate._x000D_ Unit Definition_x000D_ One unit will convert 1.0 μmole of oxalacetate and β-NADH to L-malate and β-NAD per min at pH 7.5 at 25°C._x000D_ Physical form_x000D_ Suspension in 2.8 M (NH4)2SO4 solution, pH 6.0