PDF herunterladen
Thromb Haemost 1971; 25(03): 590-595
DOI: 10.1055/s-0038-1654332
Originalarbeiten – Original Articles – Travaux Originaux
Schattauer GmbH

A Method to Study Inhibitors of Plasminogen Activation

H. D Bruhn
1   Department of Medicine, Head Prof. Dr. A. Bernsmeier, of the University of Kiel, West-Germany
› Institutsangaben
Weitere Informationen

Publikationsverlauf

Publikationsdatum:
28. Juni 2018 (online)

Auch verfügbar auf
    Lizenzen und Reprints

Summary

A method to study inhibitors of plasminogen activation is described. It is mainly thought to be a one-stage plasminogenolytic method. The same type of inhibition is found in this one-stage assay system and in a two-stage caseinolytic assay system when epsilon aminocaproic acid and salicylic acid derivatives are investigated in parallel in both assay systems. Epsilon aminocaproic acid and salicylic acid derivatives inhibit the activation of plasminogen by urokinase in a competitive way. Alpha2-macroglobulin and antithrombin III did not inhibit the activation of plasminogen by urokinase.

 

  • References

  • 1 Alkjaersig N, Fletcher A. P, Sherry S. Epsilon aminocaproic acid: and inhibitor of plasminogen activation. J. biol. Chem 234: 832 1959;
    PubMedGoogle Scholar
  • 2 Bergstrom K, Tse A. O, Johnson A. J. Fed. Proc. 1967
    PubMedGoogle Scholar
  • 3 Bruhn H. D, Bergström K, Johnson A. J. Eine Methode zur quantitativen Bestimmung von Plasminogenaktivatoren. In: Therapeutische und experimentelle Fibrinolyse. 27 F.K. Schattauer Verlag; Stuttgart – New York: 1969. (This meeting took place in 1967.)
    Google Scholar
  • 4 Bruhn H. D, Bergström K, Johnson A. J. Unpublished data.
    PubMed
  • 5 Bruhn H. D, Müller L, Duckert F. Plasminogen- und Plasminbestimmung in Humanplasma. Schweiz, med. Wschr 98: 1650 1968;
    PubMedGoogle Scholar
  • 6 Bruhn H. D, Müller L, Duckert F. Quantitative Determination of Plasminogen. Thrombos. Diathes. haemorrh. (Stuttg.) 23: 191 1970;
    PubMedGoogle Scholar
  • 7 Bruhn H. D. Plasminogenaktivierung und intravaskuläre Gerinnung. Diskussion in »13. Tagung der Deutschen Arbeitsgemeinschaft für Blutgerinnungsforschung«, März 1969. F.K. Schattauer Verlag; Stuttgart – New York: 1971. (In print.)
    Google Scholar
  • 8 Dixon M, Webb E. G. Enzymes. Longmans; 1960
    Google Scholar
  • 9 Hoepfinger L. M, Mertz E. T. Studies on plasminogen. VII. Mechanism of activation of bovine plasminogen. Canad. J. Biochem 47: 909 1969;
    PubMedGoogle Scholar
  • 10 Johnson A. J, McCarty W. R, Tillett W. S, Tse A. O, Skoza L, Newman J, Semar M. Fibrinolytic, Caseinolytic and Biochemical Methods for the Study of Thrombolysis in Man : Application and Standardization. In: Blood Coagulation, Hemorrhage and Thrombosis. Edited by Tocantins L. M, Kazal L. K. 449 Grune and Stratton; New York – London: 1964
    Google Scholar
  • 11 Von Kaulla K. N, Ens G. On structure-related properties of synthetic organic clot-dissolving thrombolytic compounds. Biochem. Pharmacol 16: 1023 1967;
    CrossrefPubMedGoogle Scholar
  • 12 Lowry O. H, Rosebrough N. J, Farr A. J, Randall R. J. Protein measurement with the Folin Phenol Reagent. J. biol. Chem 193: 265 1951;
    PubMedGoogle Scholar
  • 13 Robbins K. G, Summaria L, Hsieh B, Shah R. J. The Peptide Chains of Human Plasmin. J. biol. Chem 242: 2333 1967;
    PubMedGoogle Scholar
  • 14 Schnitze H. E, Heimburger N, Heide K, Haupt H, Störike K, Schwick H. G. Preparation and Characterization of alpha1-Trypsin Inhibitor and alpha2-Plasmin Inhibitor of Human Serum. Proc. 9th Congr. Europ. Haemat., Lisbon 1963. S. Karger; Basel – New York: 1963
    Google Scholar
  • 15 Smith M. J. H, Gould B. J, Huggins A. K. Inhibition of glutamate decarboxylase by salicylate congeners. Biochem. Pharmacol 12: 917 1963;
    CrossrefPubMedGoogle Scholar
  • 16 Whitehouse M. W. Uncoupling of oxidative phosphorylation in a connective tissue (cartilage) and liver mitochondria by salicylate analogues: relationship of structure to activity. Biochem. Pharmacol 13: 319 1964;
    CrossrefPubMedGoogle Scholar