LDH-L, Kinetic, 10 x 6 ml

The enzyme lactate dehydrogenase (LDH-L) is distributed in tissues particularly heart, liver, muscle, and kidney. The enzyme found in circulation is a mixture of five isoenzymes based on their mobility. Elevated serum levels of LDH-L are found in serum in myocardial infarction, liver disease, renal disease, certain forms of anemia, malignant diseases, and progressive muscle dystrophy. The LDH-L enzyme activity can be measured in both directions using optimal conditions for both directions and taking into account isoenzyme variations. Assays in either direction are considered to be equivalent. However, lactate-to-Pyruvate method offers a number of advantages: (1) the rate of reaction is linear over a wide range (2) no pre-incubation is required and (3) better reagent stability. LDH catalyzes the oxidation of lactate to Pyruvate in the presence of NAD, which is subsequently reduced to NADH. The rate of NADH formation measured at 340 nm is directly proportional to serum LDH-L activity