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Thromb Haemost 1959; 3(04): 554-565
DOI: 10.1055/s-0038-1654410
DOI: 10.1055/s-0038-1654410
Originalarbeiten — Original Articles — Travaux Originaux
Fibrinolytic Activator, Glutamic Oxaloacetic Transaminase and Potassium in Myocardial Tissue at Various Stages of Human Myocardial Infarction
*) Aided by grants from Miss P. A. Braundt‘s Fund to the first author and from the Josiah Macy Jr. Foundation , New york, to Dr. Tage Astrup of the Biological Institute of the Carlsberg Foundation, Copenhagen.
Further Information
Publication History
Publication Date:
12 June 2018 (online)
Summary
1. The concentrations of GO transaminase, potassium and plasminogen activator have been estimated in tissue homogenates from different zones of 7 human myocardial infarcts of varying age.
2. Significantly decreased values for GO transaminase, plasminogen activator and potassium were found in areas with fully developed necrosis.
3. Ischemic areas showed a less marked but significant decrease in GO transaminase and potassium concentrations, whereas the plasminogen activator was normal or slightly increased.
4. Fibrosed infarcts showed increased concentrations of plasminogen activator.
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References
- 1 Albrechtsen O. K. The fibrinolytic activity of human tissues. Brit. J. Haematol 1957; 3: 284
- 2 Astrup T. Biological significance of fibrinolysis. Lancet 1956; 271: 565
- 3 Astrup T, Albrechtsen O. K. Estimation of the plasminogen activator and the trypsin inhibitor in animal and human tissues. Scand. J. clin. Lab. Invest 1957; 9: 3
- 4 Bing R. J, Castellanos A, Gradel E, LuptOn C, Siegel A. Experimental myocardial infarction. Amer. J. med. Sci 1956; 232: 533
- 5 Blumgart H. L, Gilligan D. R, Schlesinger M. J. Experimental studies on the effect of temporary occlusion of coronary arteries. Amer. Heart J 1941; 22: 374
- 6 Henley K. S, Pollard H. M. A new method for the determination of glutamic-oxaloacetic transaminase and glutamic pyruvic transaminase in plasma. J. Lab. clin. Med 1955; 46: 785
- 7 Jennings R. B, Crout J. R, Smellers G. W. Studies on distribution and localization of potassium in early myocardial ischemic injury. Arch. Path. (Chicago) 1957; 63: 586
- 8 Jennings R. B, Kaltenbach J. P, Smetters G. W. Enzymatic changes in acute myocardial ischemic injury. Arch. Path. (Chicago) 1957; 64: 10
- 9 Karmen A. A note on the spectrophotometric assay of glutamic oxaloacetic transaminase activity in human serum. J. clin. Invest 1955; 34: 131
- 10 Kattus A. A, Watanabe R, Semenson C. Diagnostic and prognostic significance of serum transaminase levels in coronary occlusive disease. Circulation (N. Y.) 1957; 15: 502
- 11 Kent S. P. Effect of post mortem autolysis on certain histochemical reactions. Arch. Path. (Chicago) 1957; 64: 17
- 12 Lunseth J. H, Ruwalt M. Pathogenesis of cardiac rupture due to myocardial infarction. Dis. Chest 1956; 30: 499
- 13 Mallory G. K, White P. D, Salcedo S. J. The speed of healing of myocardial infarction. Amer. Heart J 1939; 18: 647
- 14 Nydick I, Wroblewski F, La Due J. S. Evidence for increased serum glutamic oxaloacetic transaminase. Circulation (N. Y.) 1955; 12: 161
- 15 Rodeck H. Der Kalium-Inhalt im kranken Muskel. Schweiz. med. Wschr 1953; 83: 1137
- 16 Siegel A, Bing R. J. Plasma enzyme activity in myocardial infarction in dog and man. Proc. Soc. exp. Biol. (N. Y.) 1956; 91: 604
- 17 Tennant R, Grayzel D. M, Sutherland F. A, Stringer S. W. Studies on experimental coronary occlusion. Chemical and anatomical changes in the myocardium after coronary ligation. Amer. Heart J 1936; 12: 168
- 18 Wallace W. M. The application of the internal standard flame photometer to the analysis of biological material. J. Lab. clin. Med 1951; 37: 621
-
References
- 1 Albrechtsen O. K. The fibrinolytic activity of human tissues. Brit. J. Haematol 1957; 3: 284
- 2 Astrup T. Biological significance of fibrinolysis. Lancet 1956; 271: 565
- 3 Astrup T, Albrechtsen O. K. Estimation of the plasminogen activator and the trypsin inhibitor in animal and human tissues. Scand. J. clin. Lab. Invest 1957; 9: 3
- 4 Bing R. J, Castellanos A, Gradel E, LuptOn C, Siegel A. Experimental myocardial infarction. Amer. J. med. Sci 1956; 232: 533
- 5 Blumgart H. L, Gilligan D. R, Schlesinger M. J. Experimental studies on the effect of temporary occlusion of coronary arteries. Amer. Heart J 1941; 22: 374
- 6 Henley K. S, Pollard H. M. A new method for the determination of glutamic-oxaloacetic transaminase and glutamic pyruvic transaminase in plasma. J. Lab. clin. Med 1955; 46: 785
- 7 Jennings R. B, Crout J. R, Smellers G. W. Studies on distribution and localization of potassium in early myocardial ischemic injury. Arch. Path. (Chicago) 1957; 63: 586
- 8 Jennings R. B, Kaltenbach J. P, Smetters G. W. Enzymatic changes in acute myocardial ischemic injury. Arch. Path. (Chicago) 1957; 64: 10
- 9 Karmen A. A note on the spectrophotometric assay of glutamic oxaloacetic transaminase activity in human serum. J. clin. Invest 1955; 34: 131
- 10 Kattus A. A, Watanabe R, Semenson C. Diagnostic and prognostic significance of serum transaminase levels in coronary occlusive disease. Circulation (N. Y.) 1957; 15: 502
- 11 Kent S. P. Effect of post mortem autolysis on certain histochemical reactions. Arch. Path. (Chicago) 1957; 64: 17
- 12 Lunseth J. H, Ruwalt M. Pathogenesis of cardiac rupture due to myocardial infarction. Dis. Chest 1956; 30: 499
- 13 Mallory G. K, White P. D, Salcedo S. J. The speed of healing of myocardial infarction. Amer. Heart J 1939; 18: 647
- 14 Nydick I, Wroblewski F, La Due J. S. Evidence for increased serum glutamic oxaloacetic transaminase. Circulation (N. Y.) 1955; 12: 161
- 15 Rodeck H. Der Kalium-Inhalt im kranken Muskel. Schweiz. med. Wschr 1953; 83: 1137
- 16 Siegel A, Bing R. J. Plasma enzyme activity in myocardial infarction in dog and man. Proc. Soc. exp. Biol. (N. Y.) 1956; 91: 604
- 17 Tennant R, Grayzel D. M, Sutherland F. A, Stringer S. W. Studies on experimental coronary occlusion. Chemical and anatomical changes in the myocardium after coronary ligation. Amer. Heart J 1936; 12: 168
- 18 Wallace W. M. The application of the internal standard flame photometer to the analysis of biological material. J. Lab. clin. Med 1951; 37: 621