General description
L-Lactic Dehydrogenase (LDH) is present in the cell cytoplasm and is part of the glycolytic pathway. It exists in different isoforms in heart and muscles. LDH is a tetramer corresponding to a molecular weight of 140 kDa. LDH has a nucleotide-cofactor binding site and has the structure of Rossmann fold.
Application
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).
Biochem/physiol Actions
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.
Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids.
Unit Definition
One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.
Physical form
Solution in 50% glycerol containing 0.025 M potassium phosphate buffer, pH 7.5
Analysis Note
Protein determined by biuret