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Original Article

Fibrinolysis and the Bovine Lung Trypsin Inhibitor (“Pulmin”)

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Pages 567-576 | Received 25 Mar 1966, Published online: 08 Jul 2009

References

  • Amris C. J. Inhibition of fibrinolysis and thrombo-plastic activity by Trasylol®. Xth Cong. Inter-nat. Soc. Haematol., Stockholm, 1964, Abstract G:72
  • Anderer F. A. Strukturuntersuchungen am Kalli-krein-Inactivator aus Rinderlunge. II. Be-stimmung der Aminosauresequenz. Zschr. f. Naturwissenschaften 1965; 20b: 462
  • Astrup T. A proteolytic inhibitor in lung tissue. 18th Internat. Physiol. Congr., Copenhagen, 1950; 81, Abstracts
  • Astrup T. Ox lung tissue as a proteolytic inhibitor. Acta physiol. scand. 1952; 26: 243
  • Astrup T., Egeblad K. Thrombelastographic patterns produced by fibrinolytic agents incorporated in fibrin. Amer. J. Physiol. 1965; 209: 84
  • Astrup T., Nissen U. Urinary trypsin inhibitor (Mingin) : Transformation into a new trypsin inhibitor by acid hydrolysis or by sialidase. Nature 1964; 203: 255
  • Astrup T., Stage A. A protease inhibitor in ox lung tissue. Acta chem. scand. 1956; 10: 617
  • Beck E., Schmutzler R., Duckert F. Inhibition of fibrinolysis and fibrinogenolysis in man: comparison of ϵ-aminocaproic acid and kalli-krein inhibitor. Thrombos. Diathes. haemorrh. 1963; 10: 106
  • Blix S. The euglobulin method for estimation of fibrinolytic activity in urokinase-activated plasma and the influence of Trasylol®. Scand. J. clin. Lab. Invest. 1964; 16: 198
  • Deutsch E., Fischer M. Kinetics of the inhibition of plasmin by trypsin inhibitors. Proc. 9th Cong. Europ. Soc. Haematol., Lisbon. Karger, Basel 1963; 1321
  • Egeblad K. Effects of epsilon-aminocaproic acid on fibrin clot lysis. Thrombos. Diathes. hae-morrh. 1966a; 15: 173
  • Egeblad K. Effect of soy bean trypsin inhibitor on fibrin clot lysis. Thrombos. Diathes. hae-morrh. 1966b; 15: 542
  • Astrup T., Astrup T. Fibrinolysis and the trypsin inhibitor in human urine. Scand. J. clin. Lab. Invest. 1966; 18: 1
  • Herschlein H. J., Steichele D. F. Die Hem-mung der Hyperkoagulabilität des Blutes. Med. Welt. 1964; 1314
  • Kassell B., Laskowski M. The basic trypsin inhibitor of bovine pancreas. V. The disulfide linkages. Biochem. biophys. Res. Commun. 1965; 20: 463
  • Kjeldgaard N. O., Ploug J. Urokinase, an activator of plasminogen from human urine. II. Mechanism of plasminogen activation. Biochim. biophys. Acta 1957; 24: 283
  • Kraut H., Bhargava N. Versuche zur Isolierung des Kallikrein-Inaktivators. V. Isolierung eines Kallikrein-Inaktivators aus Rinderlunge und seine Identifizierung mit dem Inaktivator aus Rinderparotis. Zschr. Physiol. Chem. 1964; 338: 231
  • Kraut H., Bhargava N., Korbel-Enkhardt R. Versuche zur Isolierung des Kallikrein-Inaktivators. Zschr. Physiol. Chem. 1958; 312: 161
  • Marx R., Clemente P., Werle E., Appel W. Über die Wirkung von Proteinaseinhibitor-Präparaten (Leber- und Parotis-inhibitor) auf die extravasale Fibrinolyse, Fibrinogenolyse und Blutgerinnungskonstanten im Menschenblut. Blut 1963; 9: 164
  • Nissen U., Astrup T. Purity and specific activity of plasmin preparations determined with inhibitors. Fed. Proc. 1966; 25: 193, Abstract No. 30
  • Sherry S., Alkjaersig N. Studies on the fibrinolytic enzyme of human plasma. Thrombos. Diathes. haemorrh. 1957; 1: 264
  • Soulier J. P., Prou-Wartelle O., Dormont J. Etude de diverse inhibiteurs d'enzymes proteo-lytiques sur la coagulation et la fibrinolyse. Rev. Hémat. 1960; 15: 431
  • Waldmann-Meyer H., Nielsen E., Astrup T. (1962) Comparative study of the trypsin inhibitors from ox-lung, pancreas, and human urine. Proc. 8th Congr. Europ. Soc. Haematol., Vienna, 1961. Karger, Basel, Comm. No. 456
  • Werle E., Appel W. Isolierung eines natür-lichen Inactivators für Kallikrein und einigen Proteinasen aus Rinderleber. Naturwissen-schaften 1958; 45: 60

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