L-Lactic Dehydrogenase from bovine muscle

Protein determined by biuret.

L-Lactic Dehydrogenase from bovine muscle has been used in lactate assay to assess lactate tissue accumulation.

Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids.

Lactate dehydrogenase (LDH) plays a critical role as a checkpoint in gluconeogenesis and DNA metabolism. It plays a vital role in maintaining homeostasis during periods of low oxygen availability. As an oxidoreductase enzyme, lactate dehydrogenase catalyzes the reversible conversion of pyruvate to lactate using NADH. This enzyme is crucial for the anaerobic metabolism of glucose when oxygen is either absent or in short supply. LDH is the sole serum biomarker effective for evaluating metastatic melanomas.

Research Area: Cell Signaling
Lactate dehydrogenase (LDH) is a key enzyme in the anaerobic metabolic pathway and falls under the class of oxidoreductases. This enzyme is found in a wide range of organisms, including both plants and animals. It is widely distributed across all tissues. LDH is primarily a cytoplasmic enzyme, with particularly high concentrations in muscle, liver, and kidney tissues.

One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.

Crystalline suspension in 2.4 M (NH₄)₂SO₄ solution, pH 6.0