Thrombosis and Haemostasis, Table of Contents Thromb Haemost 1971; 25(03): 590-595DOI: 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 › Author Affiliations Recommend Article Abstract Buy Article 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. Full Text References References 1 Alkjaersig N, Fletcher A. P, Sherry S. Epsilon aminocaproic acid: and inhibitor of plasminogen activation. J. biol. Chem 234: 832 1959; 2 Bergstrom K, Tse A. O, Johnson A. J. Fed. Proc. 1967 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 (This meeting took place in 1967.) 4 Bruhn H. D, Bergström K, Johnson A. J. Unpublished data. 5 Bruhn H. D, Müller L, Duckert F. Plasminogen- und Plasminbestimmung in Humanplasma. Schweiz, med. Wschr 98: 1650 1968; 6 Bruhn H. D, Müller L, Duckert F. Quantitative Determination of Plasminogen. Thrombos. Diathes. haemorrh. (Stuttg.) 23: 191 1970; 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.) 8 Dixon M, Webb E. G. Enzymes. Longmans; 1960 9 Hoepfinger L. M, Mertz E. T. Studies on plasminogen. VII. Mechanism of activation of bovine plasminogen. Canad. J. Biochem 47: 909 1969; 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 11 Von Kaulla K. N, Ens G. On structure-related properties of synthetic organic clot-dissolving thrombolytic compounds. Biochem. Pharmacol 16: 1023 1967; 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; 13 Robbins K. G, Summaria L, Hsieh B, Shah R. J. The Peptide Chains of Human Plasmin. J. biol. Chem 242: 2333 1967; 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 15 Smith M. J. H, Gould B. J, Huggins A. K. Inhibition of glutamate decarboxylase by salicylate congeners. Biochem. Pharmacol 12: 917 1963; 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;
