Merck, 59747-100MG, Lactic Dehydrogenase, recombinant from E. coli

General description
LDH (lactic dehydrogenase), a glycolytic enzyme, particularly present in skeletal muscle, heart, liver, kidneys, brain, lungs and red blood cells. It has five isoenzyme forms. LDH possess a tetrameric structure.
Application
Lactic Dehydrogenase, recombinant from E. coli has been used:
in lactate dehydrogenase (LDH) and malate dehydrogenase 1 (MDH1)assays and cross-linking assays
to prepare assay buffer to measure pyruvate kinase (PYK) by coupled assay
in in vitro DltC D-alanylation assay

Biochem/physiol Actions
L-lactic dehydrogenase catalyzes the conversion of L-lactate into L-pyruvate while reducing NAD+ to NADH and H+.
Conversion of L-lactate into L-pyruvate is crucial in hypoxic and anaerobic conditions, especially when synthesis of adenosine triphosphate (ATP) by oxidative phosphorylation is interrupted.
Other Notes
One unit corresponds to the amount of enzyme which reduces 1 μmol pyruvate per minute at pH 7.4 and 25°C (NADH as cofactor)