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Clinical Chemistry 18: 275-279, 1972;
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Clinical Chemistry, Vol 18, 275-279, Copyright © 1972 by the American Association for Clinical Chemistry

"Glycerate Dehydrogenase" Activity in Acute Myocardial Infarction and Myocardial Ischemia

M. J. McQueen 1, I. W. C. Garland 1, and H. G. Morgan 1

1 Cardiac Surgery Unit and the Department of Biochemistry, Royal Infirmary, Glasgow, U.K.

Hydroxypyruvate has been shown to be an alternative substrate for lactate dehydrogenase. The clinical value of this "glycerate dehydrogenase" has been investigated on 60 patients admitted to the hospital with a provisional diagnosis of myocardial infarction. For comparison, lactate dehydrogenase, agr-hydroxybutyric dehydrogenase, creatine kinase, aspartate transaminase, and alanine transaminase were also assayed at 37°C. Normal ranges and methods of assay are given for each enzyme. Glycerate dehydrogenase has greater activity than any other enzyme and parallels lactate dehydrogenase and agr-hydroxybutyric dehydrogenase in its time of peak activity and duration of increased activity. Clinical and biochemical evidence is provided to show that agr-hydroxybutyric dehydrogenase is not specific for the cardiac isoenzymes. Of the enzymes studied, creatine kinase activity increases most quickly after myocardial infarction, and an exclusive role for its use in coronary care units is also suggested.


Key Words: lactate dehydrogenase • agr-hydroxybutyric dehydrogenase • creatine kinase • aspartate transaminase • glutamic-oxaloacetate transaminase • alanine transaminase • infarction • normal values • ischemia • diagnostic aid • isoenzyme specificity

Submitted on November 17, 1971
Accepted on December 14, 1971






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Copyright © 1972 by the American Association for Clinical Chemistry.