Centrifuge specimen. Serum samples in non-gel tubes should be separated from cells promptly.
Usual
Lactate dehydrogenase is a widespread cytosolic enzyme, found in the greatest concentrations in heart, skeletal muscle, liver, kidney and red blood cells. Many of these tissues rely on anaerobic glycolysis for energy. LDH catalyses the conversion of pyruvate to lactate, and vice versa. In the forward reaction, NADH is oxidized to produce NAD. NAD is vital as an oxidizing agent to facilitate flux through the glycolytic pathway. Increased plasma activity is usually the result of leakage of enzyme from tissues as a result of damage: it is 500 times more concentrated within the cytosol relative to plasma. LDH is a tetramer made up of combinations of 2 polypeptide chains. Five isoenzymes are recognised, designated LD1 to LD5, according to the number of each chain type resulting in different molecular mass and electrophoretic mobility:
Following a myocardial infarction:
Therefore, LDH was thought to provide a valuable late indicator of infarction. It is however not often used in this context in current practice.
LDH may also be raised in:
None
Analysis CANNOT be performed on specimens that have been refrigerated or frozen.
Haemolysis interferes with this method
Please note Isoenzyme analysis is not available
125 - 220 U/L
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Tests not appearing on the UKAS Schedule of Accreditation currently remain outside of our scope of accreditation. However, these tests have been validated to the same high standard as accredited tests and are performed by the same trained and competent staff.
For further test information, please visit the test database: http://qehbpathology.uk/test-database
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