Principle of the Procedure

Lactate dehydrogenase (LDH) is an oxidoreductase (EC 1.1.1.27) presents in a wide variety of organisms. It catalyses the inter-conversion of pyruvate and lactate with concomitant inter-conversion of NADH and NAD+. It converts pyruvate, the final product of glycolysis, to lactate in hypoxic conditions. LDH quantification is of clinical interest as serum levels of certain LDH isozymes reflect pathological conditions in particular tissues. When disease or injury or toxic material damages tissues, the cells LDH is released into the bloodstream. Since LDH is a fairly stable enzyme, LDH has been widely used to evaluate the presence of damage and toxicity of tissue and cells. The kit provides a simple and easy colorimetric assay for measuring Lactate Dehydrogenase in Animal and Plant Tissues, Cells, Plasma, Serum and other biological fluids. The principle is that LDH catalyzes NAD+ to oxidize lactic acid to produce pyruvate, and pyruvate further reacts with 2, 4-dinitrophenylhydrazide to produce pyruvate dinitrophenylhydrazone,which is brown-red in alkaline solution and has the maximum absorption peak at 520 nm. In a certain concentration range, the pyruvate content is proportional to the absorbance of 520nm. According to the standard curve, the content of pyruvate in the sample can be calculated, and then reflect the LDH activity.