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Serum Beta-enolase in Acute Myocardial Infarction

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Journal Br Heart J
Date 1987 Jul 1
PMID 3620239
Citations 6
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Abstract

The enzyme beta-enolase (alpha beta and beta beta forms) is present in skeletal and heart muscle and catalyses the glycolysis of 2-phosphoglycerate to phosphoenolpyruvate. The enzyme was measured in serum samples from patients with acute myocardial infarction, angina pectoris, congestive heart failure, and idiopathic cardiomyopathy. Serum concentrations of beta-enolase were significantly increased in acute myocardial infarction but not in the other cardiovascular diseases. Activity peaked approximately 12 to 14 hours after an acute attack of chest pain, and then gradually decreased as the patient recovered. The rise and fall in beta-enolase concentration were faster and steeper than those of creatine kinase activity, particularly in patients in whom activities of both these enzymes were less high. The assay of beta-enolase, which is highly specific and sensitive, has considerable advantages for the early diagnosis of myocardial infarction and the diagnosis of a second episode of myocardial infarction because beta-enolase concentration increases very early and rapidly and clears quickly. These data imply that serum beta-enolase may be a more effective marker for early myocardial infarction, particularly in milder cases, than measurement of creatine kinase activity.

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References
1.
Shaft F, BAN R, IMFELD H . Serum pyruvate kinase in acute myocardial infarction. Am J Cardiol. 1970; 26(2):143-50. DOI: 10.1016/0002-9149(70)90772-1. View

2.
Hess B . DPN-dependent enzymes in serum. Ann N Y Acad Sci. 1958; 75(1):292-303. DOI: 10.1111/j.1749-6632.1958.tb36877.x. View

3.
Wagner G, Roe C, Limbird L, Rosati R, Wallace A . The importance of identification of the myocardial-specific isoenzyme of creatine phosphokinase (MB form) in the diagnosis of acute myocardial infarction. Circulation. 1973; 47(2):263-9. DOI: 10.1161/01.cir.47.2.263. View

4.
Harano Y, Adair R, VIGNOS Jr P, Miller M, Kowal J . Pyruvate kinase isoenzymes in progressive muscular dystrophy and in acute myocardial infarction. Metabolism. 1973; 22(3):493-501. DOI: 10.1016/0026-0495(73)90041-3. View

5.
BONTE F, Parkey R, Graham K, Moore J, Stokely E . A new method for radionuclide imaging of myocardial infarcts. Radiology. 1974; 110(2):473-4. DOI: 10.1148/110.2.473. View