リンゴ酸デヒドロゲナーゼ ブタ心臓由来

1ユニットは、pH 7.5、25°C、1分間で、1.0 μmolのオキサロ酢酸とβ-NADHをL-リンゴ酸とβ-NADに変換する酵素量です。

2.8 M (NH₄)₂SO₄溶液(pH 6.0)の懸濁液

Malic Dehydrogenase from porcine heart has been used:

• in qualitative protein binding measurements
• to test internally calibrated electrochemical continuous enzyme assay (ICECEA) with model enzyme pair
• to investigate the effect of chaperone on the refolding of heat-denatured malate dehydrogenase

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.

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.

Malic Dehydrogenase is a ubiquitous enzyme, which exists in two isoforms in eukaryotic cells.

Malic dehydrogenase exists as a dimer with each subunit containing an NAD-binding domain and a substrate-binding carboxy-terminal domain required for activity.

Malic dehydrogenase is a cytoplasmic isozyme and an important catalyst in the tricarboxylic acid cycle.