LDH-P

200

Enzymes

Lactate dehydrogenase (LDH)

Fresh non-haemolysed serum

R1: 3 x 12.6 mL;
R2: 1 x 4.4 mL,
Ready to use

Instructions for Use  |  Safety Data Sheet

For professional use only.

LDH is an enzyme which catalyses the reduction of pyruvic acid to lactic acid. The wide-spread diffusion of LDH in the organism explains why this enzyme increases in the serum in numerous pathological conditions involving various tissues, such as the liver (viral hepatitis), cardiac muscle (myocardial infarction), skeletal muscle and kidneys. The kidney is the organ containing the highest concentration of the enzyme, followed by the myocardium, skeletal muscle, spleen, liver and lungs. LDH activity in the serum is determined by a group of five isoenzymes deriving from different tissues. LDH activity can be determined by measuring the conversion of lactate to pyruvate or pyruvate to lactate. Hill and Levi in 1954, Wròblewski and La Duein 1956, and Blachaer in 1961 developed methods based on the use of NADH. The method has been optimised according to the suggestions proposed by the Scandinavian Society for Clinical Chemistry (1).

LDH catalyses the following reaction:
pyruvate + NADH + H+ --(LDH)--> lactate + NAD+
The rate of NADH oxidation is proportional to the LDH activity.

Store at 2 - 8°C and protect from direct light. When correctly stored, the reagents are stable up to the expiry date reported on the label. A slight variation in the composition of the reagents may occur between batches, but this has no effect on the test results. After opening, the vial R1 and R2 are stable 30 days if recapped immediately and protected from contamination, evaporation, direct light and stored at correct temperature.

Multicalibrator (R0300000006)
Normal control serum (R0400000006)
Pathological control serum (R0400000106)