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.
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).
L-Lactic dehydrogenase is used in the determination of pyruvate (used in conjunction with reduced coenzyme) and in the diagnosis of myocardial infarction and leukemia.
L-lactate dehydrogenase (LDH) is an enzyme that catalyzes the conversion of lactate to pyruvate.?In particular, lactic dehydrogenase A (LDHA) is mainly found in skeletal muscle, and for that reason is known as the M subunit. This recombinant form of LDHA has a C-terminal histidine-tag.
The gene LDHA (L-lactate dehydrogenase A chain) is mapped to human chromosome 11p15. It is a subunit of lactate dehydrogenase.
Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids.
A forty-fold purification of the dehydrogenase is effected by affinity chromatography using Sepharose 4B coupled to 8-(6-aminohexyl)amino-5'-AMP or -NAD . [Lees et al. Arch Biochem Biophys 163 561 1974, Pesce et al. J Biol Chem 239 1753 1964.]
