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59747 Sigma-Aldrich

Lactic Dehydrogenase, recombinant from E. coli

≥90 U/mg

Synonym: (S)-Lactate: NAD+ oxidoreductase, L-Lactate Dehydrogenase, Lactate

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Description

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

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.

L-lactic dehydrogenase catalyzes the conversion of L-lactate into L-pyruvate while reducing NAD+ to NADH and H+.

Unit Definition

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)

Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
3

Documents

Certificate of Analysis

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Protocols & Articles

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Metabolomics, Molecular biology

Peer-Reviewed Papers
15

References

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