Clinical Pathology: General Principles, Clinical Chemistry

• LDH has a molecular mass of about 135,000 Da and is a tetramer composed of heart (H) and muscle (M) subunits, which give rise to five isoenzymes. The LDH-1 (H4) isoenzyme is found mainly in heart, brain, and erythrocytes; the LDH-2 (H3M) is found in myocardium; and the LDH-5 isoenzyme predominates in the liver and skeletal muscle.

• In normal serum, LDH-2 is the most common isoenzyme, and the LDH-1/LDH-2 ratio is usually less than 1. The LDH-1 fraction will be greater than the LDH-2 fraction (i.e., “a flipped LDH-1/LDH-2 pattern”) if (1) hemolysis is present or (2) it has been several days since an acute myocardial infarction.

• Haptoglobin is an acute-phase protein. Haptoglobin levels are decreased when there is hemolysis because the released hemoglobin binds haptoglobin and is rapidly cleared from the circulation.

• During hemolysis, significant amounts of LDH-1 isoenzyme are released from the erythrocytes, resulting in a flipped LDH-1/LDH-2 pattern.

• A flipped LDH-1/LDH-2 pattern is not a specific marker for myocardial necrosis.

Bruns DE, Emerson JC, Intemann S, et al: Lactate dehydrogenase isoenzyme 1: changes in the first day after acute myocardial infarction. Clin Chem 1981; 27: 1821–1823.

Rotenberg Z, Seif R, Wolfe LA, et al: Flipped patterns of lactate dehydrogenase isoenzymes in serum of elite basketball players. Clin Chem 1988;34:2351–2354.

 
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