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Lactate dehydrogenase in the blood
Last reviewed: 23.04.2024
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Reference values (norm) of activity of total lactate dehydrogenase in serum are 208-378 IU / l.
Lactate dehydrogenase, a glycolytic zinc-containing enzyme that reversibly catalyzes the oxidation of L-lactate to pyruvic acid, is widely distributed in the human body. The greatest activity of lactate dehydrogenase is found in the kidneys, heart muscle, skeletal muscles and liver. Lactate dehydrogenase is contained not only in the serum, but also in a significant amount in erythrocytes, so the serum for the study should be free of traces of hemolysis. Most human organs and tissues contain five isoenzymes of lactate dehydrogenase. The nature of the isoenzyme spectrum of LDH and the type of metabolism in the tissue correlate with each other. In tissues with predominantly aerobic metabolism (heart, brain, kidneys), isoenzymes LDH 1 and LDH 2 predominate . In tissues with pronounced anaerobic metabolism (liver, skeletal muscle), isoenzymes LDH 4 and LDH 5 predominate . In the serum of a healthy person, all five isoenzymes of LDH are constantly detected. A regularity is observed with respect to the activity of lactate dehydrogenase isoenzymes: LDH activity 2 > LDH 1 > LDH 3 > LDH 4 > LDH 5. Damage to one or another organ changes the isoenzymatic spectrum of blood serum, and these changes are caused by the specific isoenzymatic composition of the injured organ.
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