L-Lactic Dehydrogenase from bovine heart

Research area: Cell signaling

Lactate dehydrogenase (LDH) is a cytoplasmic enzyme that belongs to the oxidoreductase’s family. It is ubiquitously expressed in body tissues but at high levels in muscle, liver, and kidney. LDH exists as tetramer and comprises of two subunits (H and M). The LDH of eukaryotes undergo active-site loop gating for their catalytic functionality. L-lactate, which is the major enantiomeric form of lactate in vertebrates, is produced by the L-isomers of LDH enzyme encoded by the LDHC gene.

L-Lactic Dehydrogenase from bovine heart has been used as a standard in cytotoxicity assay. It has also been used in glutamic pyruvic transaminase (GPT) assay.

Lactate dehydrogenase (LDH) is a crucial enzyme that plays a vital role in the anaerobic metabolic pathway. It facilitates the conversion of lactate to pyruvate and NAD⁺ to NADH, and vice versa, within cells. This enzymatic reaction plays a crucial role in cellular energy production, particularly in environments with low oxygen levels or hypoxic conditions. LDH activity is also significant in tumor glycolysis and the Warburg effect. LDH is released into the bloodstream when the cells are damaged or undergo death. Therefore, LDH can be used as a potential marker of cell injury and death. High lactate dehydrogenase activity is associated with various medical conditions, such as liver disease, anemia, heart attack, bone fractures, muscle trauma, and certain types of cancer.

Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids.

One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.

Crystalline suspension in 2.1 M (NH₄)₂SO₄ solution, pH 6.0

Protein determined by biuret