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Alpha HBDH

Alpha HBDH Test
Lactate dehydrogenase in serum is composed of 5 isoenzymes. These enzymes are present in a tetrameric structure. There are two types of subunits, namely the M-subunit predominantly found in skeletal muscle, and the H-subunit, found predominatly in the myocardium. Due to their electrophoretic migration characteristics to the anode, the isoenzymes are termed LDH1, LDH2, LDH3, LDH4 and LDH5. LDH1 migrates most rapidly to the anode. The subunits are composed accordingly: H4, H3M, H2M2, HM3 and M4. By using various substrates (e.g. ��-ketobutyrate is used for ��-HBDH ), lactate dehydrogenases from the liver and the heart can be differentiated from each other.

Each organ is associated with a characteristic enzyme pattern which can contribute to the identification of organ damage. Recent studies have shown that changes in the proportion of heart-specific LDH isoenzyme activities to the total LDH activity yield a reliable indication of the severity and progress of a recent myocardial infarction.2,3 Rudolph et al.4 report that the combination of CK-MB- and heart-specific LDH isoenzyme determinations can predict with 99% certainty the classification of a myocardial infarction as being acute or non-acute. Rotenberg et al5,6 report also that the measurement of heart-specific LDH isoenzymes 24 to 48 hours after heart surgery is a meaningful test for the diagnosis of perioperative myocardial infarction. This method is in accordance with the optimized standard method as recommended by the German Society for Clinical Chemistry in 1972.7

Intended use
Enzymatic in vitro test for the quantitative determination of α-hydroxybutyrate dehydrogenase (lactate dehydrogenase-1-isoenzyme) in human serum and plasma

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