L-Lactic Dehydrogenase from bovine heart

Research area: Cell signaling. L-LacticDehydrogenase (LDH) is present in the cell cytoplasm. and is part of the glycolytic pathway. Lactate dehydrogenase (LDH) is a ubiquitous molecule found in plants, yeast, mammals, and microorganisms and is a member of the oxidoreductase family. It has five isozymes (LD₁ to LD₅) and this composition varies in different tissues. LD₁ is present at higher concentrations in the heart, kidneys, and erythrocytes. LD₅ is found in the liver and skeletal muscles.(2)

L-Lactic Dehydrogenase from bovine heart has been used in ATPase assay of R2 complex Rvb1p-Rvb2p, RecA protein and sarcoplasmic reticulum Ca²⁺-ATPase (SERCA).

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

Variation in the levels of L-Lactic Dehydrogenase (LDH) isoform is a diagnostic marker for tissue damage. The levels of LDH is useful in detecting dairy cattle disease, Mastitis. Dye based purified LDH from bovine heart has analytical applications.Lactic dehydrogenase (LDH)plays an essential role in the glycolytic pathway where it is involved in the conversionof pyruvate to lactate using NAD⁺as a co-factor. It is considered an important molecule that can be used incancer therapy as it acts as a glycolytic inhibitor. Inhibition of LDH isassociated with blocking of aerobic glycolysis in the tumour cells.

Solution in 50% glycerol containing 0.025 M potassium phosphate buffer, pH 7.5

Protein determined by biuret

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