Lactic dehydrogenase (LDH) catalyzes the conversion of lactate to pyruvate in anaerobic glycolysis. It 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-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.
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