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Description_x000D_
General description_x000D_
LDH (lactic dehydrogenase) is a glycolytic enzyme. It is found in skeletal muscle, heart, liver, kidneys, brain, lungs and red blood cells. It comprises of five isoenzyme forms. LDH possess a tetrameric structure._x000D_
Application_x000D_
L-Lactic Dehydrogenase from bovine heart has been used:_x000D_
• as a reference standard to measure the LDH (lactic dehydrogenase)_x000D_
• to quench protein-bound NADH in cells_x000D_
• to measure the lactate released by the cells in suspension_x000D_
Packaging_x000D_
2.5 mL in glass bottle_x000D_
Biochem/physiol Actions_x000D_
LDH (lactic dehydrogenase) helps in the reversible conversion of lactate to pyruvate._x000D_
Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids._x000D_
Unit Definition_x000D_
One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C._x000D_
Physical form_x000D_
Suspension in 2.2 M ammonium sulfate
- Related Categories 1.1.x.x Acting on hydroxyl groups, 1.x.x.x Oxidoreductases, Biochemicals and Reagents, Cell Biology, Enzyme Class Index, Enzymes, Inhibitors, and Substrates, Glycolysis, Glycolysis Enzymes, Metabolic Pathways, MetabolomicsMore... Quality Level