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Hamostaseologie 1986; 06(04): 148-156
DOI: 10.1055/s-0038-1655153
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Schattauer GmbH

Thrombolytika der dritten Generation

C. Korninger
1   1. Medizinischen Universitätsklinik Wien (Vorstand: Prof. Dr. Dr. h. c. E. Deutsch)
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Publication Date:
25 June 2018 (online)

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  • Literatur

  • 1 Nolf R. Contribution a l’etude de la coagulation du sang (5ieme memoire). La fibrinolyse. Arch Int Physiol 1905; 06: 306.
    PubMedGoogle Scholar
  • 2 Tillet W S, Johnson A J, McCarthy W R. The intravenous infusion of the streptococcal fibrinolytic principal (streptokinase) into patients. J Clin Invest 1955; 34: 169.
    CrossrefPubMedGoogle Scholar
  • 3 Moser K M. Effects of intravenous administration of fibrinolysin (plasmin) in man. Circulation 1959; 20: 42.
    CrossrefPubMedGoogle Scholar
  • 4 Karaca M, Stefanini M, Meie R. Fibrinolysis VII. Clot lysis, coagulation, and fibrinolytic mechanisms after administration of Aspergillin 0 (mold fibrinolysin) in man. J Lab Clin Med 1962; 59: 799-814.
    PubMedGoogle Scholar
  • 5 Deutsch E, Fischer M. Die Wirkung intravenös applizierter Streptokinase auf Fibrinolyse und Blutgerinnung. Thromb Diath Haemorrh 1960; 04: 482-506.
    PubMedGoogle Scholar
  • 6 Hansen P F, Jorgensen M, Kjeldgaard N O, Ploug J. Urokinase an activator of plasminogen from human urine. Experiences with intravenous application on twenty-two patients. Angiology 1961; 12: 367-71.
    CrossrefPubMedGoogle Scholar
  • 7 Sherry S, Gustafson E. The current and future use of thrombolytic therapy. Ann Rev Pharmacol Toxicol 1985; 25: 413-31.
    CrossrefPubMedGoogle Scholar
  • 8 Lijnen H R, Collen D. Interaction of plasminogen activators and inhibitors with plasminogen and fibrin. Semin Thromb Haemostas 1982; 08: 2-10.
    Article in Thieme ConnectPubMedGoogle Scholar
  • 9 Collen D. On the regulation and control of fibrinolysis. Thromb Haemostas 1980; 43: 77-89.
    PubMedGoogle Scholar
  • 10 Pennica D, Holmes W E, Kohr W J, Harkins R N, Vehar G A, Ward C A, Bennett W F, Ylverton E, Seeburg P H, Heyneker H L, Goeddel D V, Collen D. Cloning and expression of human tissue-type plasminogen activator cDNA in E. coli. Nature 1983; 301: 214-21.
    PubMedGoogle Scholar
  • 11 Ranby M. Tissue plasminogen activator. Isolation, enzymatic properties and assay procedure. Thesis, Umea University Medical Dissertation; New Series, No. 70, Umea 1982
    Google Scholar
  • 12 Albrechtsen O K. The fibrinolytic activity of human tissues. Brit J Haematol 1957; 03: 284-91.
    CrossrefPubMedGoogle Scholar
  • 13 Kok P, Astrup T. Isolation and purification of a tissue plasminogen activator and its comparison with urokinase. Biochemistry 1969; 08: 79-86.
    CrossrefPubMedGoogle Scholar
  • 14 Cole E R, Bachmann F. Purification and properties of a plasminogen activator from pig heart. J Biol Chem 1977; 252: 3729-37.
    PubMedGoogle Scholar
  • 15 Rijken D C, Wijngaards G, Zaal-De-Jong M, Welbergen J. Purification and partial characterization of plasminogen activator from human uterine tissue. Biochim Biophys Acta 1979; 580: 140-53.
    CrossrefPubMedGoogle Scholar
  • 16 Binder B R, Spragg J, Austen K F. Purification and characterization of human vascular plasminogen activator derived from blood vessel perfusates. J Biol Chem 1979; 254: 1998-2003.
    PubMedGoogle Scholar
  • 17 Rijken D C, Collen D. Purification and characterization of the plasminogen activator secreted by human melanoma cells in culture. J Biol Chem 1981; 256: 7035-41.
    PubMedGoogle Scholar
  • 18 Binder B R, Spragg J. The effect of fibrin on the activity of purified human vascular plasminogen activator. In: Protides of the Biological Fluids. Vol. 28. Peeters H. (Ed). Oxford: Pergamon Press; 1980: 391-4.
    Google Scholar
  • 19 Hoylaerts M, Rijken D C, Lijnen H R, Collen D. Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin. J. Biol. Chem 1982; 257: 2912-9.
    PubMedGoogle Scholar
  • 20 Ranby M. Studies on the kinetics of plasminogen activation by tissue plasminogen activator. Biochim Biophys Acta 1982; 704: 461-9.
    CrossrefPubMedGoogle Scholar
  • 21 Beckmann R, Binder B R. Generation of a high affinity t-PA binding site in fcb-2 fibrinogen fragments by limited proteolysis. Thromb Haemostas 1985; 54: 60.
    PubMedGoogle Scholar
  • 22 Nieuwenhuizen W, Verheijen J H, Vermond A, Chang G T G. Plasminogen activation by tissue activator is accelerated in the presence of fibrin(ogen) cyanogen bromide fragment FCB-2. Biochim Biophys Acta 1983; 755: 531-3.
    CrossrefPubMedGoogle Scholar
  • 23 Zamarron C, Lijen H R, Collen D. Kinetics of the activation of plasminogen by natural and recombinant tissue-type plasminogen activator. J Biol Chem 1984; 259: 2080-3.
    PubMedGoogle Scholar
  • 24 Ranby M, Bergsdorf N, Nilsson T. Enzymatic properties of the oneand two-chain form of tissue plasminogen activator. Thromb. Res 1982; 27: 175-83.
    CrossrefPubMedGoogle Scholar
  • 25 Korninger C, Stassen J M, Collen D. Turnover of human extrinsic (tissue-type) plasminogen activator in rabbits. Thromb Haemostas 1981; 46: 658-61.
    PubMedGoogle Scholar
  • 26 Fletcher A P, Biederman O, Moore D, Alkjaersig N, Sherry S. Abnormal plasminogen-plasmin system (fibrinolysis) in patients with hepatic cirrhosis: Its cause and consequences. J Clin Invest 1964; 43: 681-95.
    CrossrefPubMedGoogle Scholar
  • 27 Korninger C, Collen D. Thrombolyse mit dem Plasminogenaktivator vom Gewebetyp: Theoretische Grundlagen und tierexperimentelle Ergebnisse. In: Haemostase, Thrombophilie und Arteriosklerose. van de Loo J, Asbeck F. (Hrsg). Stuttgart New York: Schattauer: 1982: 327-30.
    Google Scholar
  • 28 Matsuo O, Rijken D C, Collen D. Comparison of the relative fibrinogenolytic, fibrinolytic and thrombolytic properties of tissue plasminogen activator and urokinase in vitro. Thromb Haemostas 1981; 42: 225-9.
    PubMedGoogle Scholar
  • 29 Korninger C, Collen D. Studies on the specific fibrinolytic effect of human extrinsic (tissue-type) plasminogen activator in human blood and in various animal species in vitro. Thromb Haemostas 1981; 46: 561-5.
    PubMedGoogle Scholar
  • 30 Lijnen H R, Marafino B J, Collen D. In vitro fibrinolytic activity of recombinant tissue-type plasminogen activator in the plasma of various primate species. Thromb Haemostas 1984; 52: 308-10.
    PubMedGoogle Scholar
  • 31 Matsuo O, Rijken D C, Collen D. Thrombolysis by human tissue plasminogen activator and urokinase in rabbits with experimental pulmonary embolus. Nature 1981; 291: 590-1.
    CrossrefPubMedGoogle Scholar
  • 32 Korninger C, Matsuo O, Suy R, Stassen J M, Collen D. Thrombolysis with human extrinsic (tissue-type) plasminogen activator in dogs with femoral vein thrombosis. J Clin Invest 1982; 69: 573-80.
    CrossrefPubMedGoogle Scholar
  • 33 Collen D, Stassen J M, Verstraete M. Thrombolysis with human extrinsic (tissuetype) plasminogen activator in rabbits with experimental jugular vein thrombosis. Effect of molecular form and dose of activator, age of the thrombus, and route of administration. J Clin Invest 1983; 71: 368-76.
    CrossrefPubMedGoogle Scholar
  • 34 Bergmann S R, Fox K A A, Ter-Pogossian M T, Sobel B E. Clot-selective coronary thrombolysis with tissue-type plasminogen activator. Science 1983; 220: 1181-2.
    CrossrefPubMedGoogle Scholar
  • 35 Gold H K, Fallon J T, Yasuda T, Leinbach R C, Khaw B A, Newell J B, Guerrero J L, Vislowsky F M, Hoyng C F, Grossbard E, Collen D. Coronary thrombolysis with recombinant human tissue-type plasminogen activator. Circulation 1984; 70: 700-7.
    CrossrefPubMedGoogle Scholar
  • 36 Van de Werf F, Bergmann S R, Fox K A A, de Geest H, Hoyng C F, Sobel B E, Collen D. Coronary thrombolysis with intravenously administered human tissue-type plasminogen activator produced by recombinant DNA technology. Circulation 1984; 69: 605-10.
    CrossrefPubMedGoogle Scholar
  • 37 Flameng W, Van de Werf F, Vanhaecke J, Verstraete M, Collen D. Coronary thrombolysis and infarct size reduction following intravenous infusion of recombinant tissuetype plasminogen activator in non-human primates. J Clin Invest 1985; 75: 84-90.
    CrossrefPubMedGoogle Scholar
  • 38 Topol E J, Ciuffo A A, Pearson T A, Dillmann J, Builder S, Grossbard E, Weisfeldt M L, Bulkley B H. Thrombolysis with recombinant tissue plasminogen activator in atherosclerotic thrombotic occlusion. J Amer Coll Cardiol 1985; 05: 85-91.
    CrossrefPubMedGoogle Scholar
  • 39 Weimar W, Stibbe J, van Seyen A J, Billiau A, De Somer P, Collen D. Specific lysis of an iliofemoral thrombus by administration of extrinsic (tissue-type) plasminogen activator. Lancet 1981; I: 1018-20.
    PubMedGoogle Scholar
  • 40 Van de Werf F, Ludbrook P A, Bergmann S R, Tiefenbrunn A J, Fox K A A, de Geest H, Verstraete M, Collen D, Sobel B E. Clot selective coronary thrombolysis with tissuetype plasmiogen activator in patients with evolving myocardial infarction. N Engl J Med 1984; 310: 609-13.
    CrossrefPubMedGoogle Scholar
  • 41 Sobel B E, Geltman E M, Tiefenbrunn A J, Jaffe A S, Spadaro J J, Ter-Pogossian M, Collen D, Ludbrook P A. Improvement of regional myocardial metabolism after coronary thrombolysis induced with tissue-type plasminogen activator or streptokinase. Circulation 1984; 69: 683-90.
    PubMedGoogle Scholar
  • 42 Verstraete M, Bernard R, Bory M, Brower R W, Collen D, de Bono D P, Erbel R, Huhmann W, Lennane R J, Lubsen J, Mathey D, Meyer J, Michels H R, Rutsch W, Schartl M, Schmidt W, Uebis R, von Essen R. Randomised trial of intravenous recombinant tissue-type plasminogen activator versus intravenous streptokinase in acute myocardial infarction. Lancet 1985; I: 842-7.
    PubMedGoogle Scholar
  • 43 The TIMI Study Group: The thrombolysis in myocardial infarction (TIMI) trial. Phase 1 findings. N Engl I Med 1985; 312: 932-6.
    PubMedGoogle Scholar
  • 44 Verstraete M, Bleifeld W, Brower R W, Charbonnier B, Collen D, De Bono D P, Dunning A J, Lennane R J, Lubsen J, Mathey D G, Michel P L, Raynaud P h, Schofer J, Vahanian A, Vanhaecke J, Van de Kley G A, Van de Werf F, Von Essen R. Doubleblind randomised trial of intravenous tissue-type plasminogen activator versus placebo in acute myocardial infarction. Lancet 1985; II: 965-9.
    PubMedGoogle Scholar
  • 45 Passamani E R, Roberts R. Clinical experience with rt-PA in the »Thrombolysis in Myocardial Infarction« trials (TIMI). Präsentation im Rahmen des Internationalen Symposiums »Facts and Hopes in Thrombolysis«. Aachen, Dezember 1985
    PubMedGoogle Scholar
  • 46 Rao Koneti A. for the TIMI Study Group: Effect of intravenous therapy with recombinant tissue plasminogen activator on plasma fibrinogen and the fibrinolytic system in patients with acute myocardial infarction (AMI). A report from the thrombolysis in myocardial infarction trial. Thromb Haemostas 1985; 54: 211.
    PubMedGoogle Scholar
  • 47 Spann J F, Sherry S, Carabello B A, Denenberg B S, Mann R H, McCann W D, Gault J H, Gentzler R D, Belber A D, Maurer A H, Cooper E M. Coronary thrombolysis by intravenous Streptokinase in acute myocardial infarction : acute and follow-up studies. Am J Cardiol 1984; 53: 655-61.
    CrossrefPubMedGoogle Scholar
  • 48 Lesuk A, Terminiello L, Traver J H. Crystalline human urokinase : some properties. Science 1965; 147: 880-2.
    CrossrefPubMedGoogle Scholar
  • 49 White W F, Barlow G H, Mozen M M. The isolation and characterization of plasminogen activators (urokinase) from human urine. Biochemistry 1966; 05: 2160-9.
    CrossrefPubMedGoogle Scholar
  • 50 Kobayashi O, Matsui K. Isolation of human urine urokinase by column chromatography on sawdust and some properties of the enzyme obtained. J Chromatogr 1981; 210: 180-5.
    CrossrefPubMedGoogle Scholar
  • 51 Holmberg L, Bladh B, Astedt B. Purification of urokinase by affinity chromatography. Biochim Biophys Acta 1976; 445: 215-22.
    CrossrefPubMedGoogle Scholar
  • 52 Ogawa H, Yamamoto H, Kalamine T, Tajima H. Purification and some properties of urokinase. Thromb Diath Haemorrh 1975; 34: 194-209.
    PubMedGoogle Scholar
  • 53 Giinzler W A, Steffens G J, Ötting F, Kim S-M A, Frankus E, Flohe L. The primary structure of high molecular mass urokinase from human urine. Hoppe-Seyler’s Z. Physiol. Chem 1982; 363: 1155-65.
    PubMedGoogle Scholar
  • 54 Steffens G J, Giinzler W A, Ötting F, Frankus E, Flohe L. The complete amino acid sequence of low molecular mass urokinase from human urine. Hoppe-Seyler’s Z Physiol Chem 1982; 363: 1043-58.
    PubMedGoogle Scholar
  • 55 Bernik M B. Increased plasminogen activator (urokinase) in tissue culture after fibrin deposition. J Clin Invest 1973; 52: 823-34.
    CrossrefPubMedGoogle Scholar
  • 56 Wun T C, Ossowski L, Reich E. A proenzyme form of human urokinase. J Biol Chem 1982; 257: 7262-8.
    PubMedGoogle Scholar
  • 57 Nielsen L S, Hansen J G, Skriver L. et al. Purification of zymogen to plasminogen activator from human glioblastoma cells by affinity chromatography with monoclonal antibody. Biochemistry 1982; 21: 6410-5.
    CrossrefPubMedGoogle Scholar
  • 58 Sumi H, Kosugi T, Matsuo O, Mihara H. Physiochemical properties of highly purified kidney cultured plasminogen activator (single polypeptide chain-urokinase). Acta Haematol Japon 1982; 45: 119-28.
    PubMedGoogle Scholar
  • 59 Husain S, Gurewich V, Lipinski B. Purification and partial characterization of a singlechain high-molecular-weight form of urokinase from human urine. Arch Biochem Biophys 1983; 220: 31-8.
    CrossrefPubMedGoogle Scholar
  • 60 Verde P, Stoppelli M P, Galeffi P, Di Nocera P. Identification and primary sequence of an unspliced human urokinase poly (A) + RNA. Proc Natl Acad Sei USA 1984; 81: 4727-31.
    CrossrefPubMedGoogle Scholar
  • 61 Kasai S, Arimura H, Nishida M, Suyama T. Primary structure of single-chain pro-urokinase. J Biol Chem 1985; 260: 12382-9.
    PubMedGoogle Scholar
  • 62 Wojta J, Kirchheimer J C, Turcu L, Christ G, Binder B R. Monoclonal antibodies against human high molecular weight urinary urokinase: Application for affinity purification of urinary prourokinase. Thromb Haemostas 1986; 55: 347-51.
    PubMedGoogle Scholar
  • 63 Heyneker H L, Holmes W E, Vehar G A. Preparation of functional human urokinase proteins. European Patent Application. nr 83103629.8, Publication nr 0092182A2, European Patent Office, Munich, West-Germany.
    PubMedGoogle Scholar
  • 64 Lijnen H R, Zamarron C, Blaber M, Winkler M E, Collen D. Activation of plasminogen by pro-urokinase. I Mechanism J Biol Chem 1986; 261: 1253-8.
    PubMedGoogle Scholar
  • 65 Collen D, Zamarron C, Lijnen H R, Hoylaerts M. Activation of plasminogen by prourokinase. II. Kinetics. J Biol Chem 1986; 261: 1259-66.
    PubMedGoogle Scholar
  • 66 Collen D, De Cock F, Lijnen H R. Biological and thrombolytic properties of proenzyme and active forms of human urokinase II. Turnover of natural and recombinant urokinase in rabbits and squirrel monkeys. Thromb Haemostas 1984; 52: 24-6.
    PubMedGoogle Scholar
  • 67 Zamarron C, Lijnen H R, van Hoef B, Collen D. Biological and thrombolytic properties of proenzyme and active forms of human urokinase I. Fibrinolytic and fibrinogenolytic properties in human plasma in vitro of urokinases obtained from human urine or by recombinant DNA technology. Thromb Haemostas 1984; 52: 19-23.
    PubMedGoogle Scholar
  • 68 Lijnen H R, De Wreede K, Demarsin E, Collen D. Biological and thrombolytic properties of proenzyme and active forms of human urokinase IV. Variability in fibrinolytic response of plasma of several mammalian species. Thromb Haemostas 1984; 52: 30-3.
    PubMedGoogle Scholar
  • 69 Sumi H, Toki N, Sasaki K, Mihara H. Comparative properties of single and double polypeptide chains of hig properties of proenzyme andh molecular weight urokinase. In: Progress in Fibrinolysis. Vol. 6. Davidson J F, Bachmann F, Bouvier C A, Kruithof E K O. (Eds). Edinburgh: Churchill Livingstone; 1983: 165-7.
    Google Scholar
  • 70 Gurewich V, Pannell R, Louie S, Kelley P, Suddith R L, Greenlee R. Effective and fibrin-specific clot lysis by a zymogen precursor form of urokinase (pro-UK). A study in vitro and in two animal species. J Clin Invest 1984; 73: 1731-9.
    CrossrefPubMedGoogle Scholar
  • 71 Collen D, Stassen J M, Blaber M, Winkler M, Verstraete M. Biological and thrombolytic properties of proenzyme and active forms of human urokinase III. Thrombolytic properties of natural and recombinant urokinase in rabbits with experimental jugular vein thrombosis. Thromb Haemostas 1984; 52: 27-9.
    PubMedGoogle Scholar
  • 72 Matsuo O, Bando H, Okada K, Tanaka K, Tsukada M, Iga Y, Arimura H. Thrombolytic effect of single-chain pro-urokinase in a rabbit jugular vein thrombosis model. Thromb Res 1986; 42: 187-94.
    CrossrefPubMedGoogle Scholar
  • 73 Collen D, Stump D, van de Werf F, Jang I K, Nobuhara M, Lijnen H R. Coronary thrombolysis in dogs with intravenously administered human pro-urokinase. Circulation 1985; 72: 384-8.
    CrossrefPubMedGoogle Scholar
  • 74 Van de Werf F, Nobuhara M, Collen D. Coronary thrombolysis with human singlechain, urokinase-type plasminogen activator (pro-urokinase) in patients with acute myocardial infarction. Ann Int Med 1986; 104: 345-8.
    CrossrefPubMedGoogle Scholar
  • 75 Smith R A G, Dupe R J, English P D, Green J. Fibrinolysis with acyl-enzymes: a new approach to thrombolytic therapy. Nature (London) 1981; 290: 505-8.
    CrossrefPubMedGoogle Scholar
  • 76 Smith R A G, Dupe R J, English P D, Green J. Acyl-enzymes as thrombolytic agents in a rabbit model of venous thrombosis. Thromb Haemostas 1982; 47: 269-74.
    PubMedGoogle Scholar
  • 77 Dupe R J, Green J, Smith R A G. Acylated derivatives of streptokinase-plasminogen activator complex as thrombolytic agents in a dog model of aged venous thrombosis. Thromb Haemostas 1985; 53: 56-9.
    PubMedGoogle Scholar
  • 78 Markwart F, Klöcking H-P, Stürzebecher J. Thrombolytic effects of acylated urokinase. Haemostasis 1984; 14: 55.
    PubMedGoogle Scholar
  • 79 Green J. Fibrinolysis with acylated streptokinase-plasminogen complex. Haemostasis 1984; 14: 83.
    PubMedGoogle Scholar
  • 80 Matsuo O, Collen D, Verstraete M. On the fibrinolytic and thrombolytic properties of active site p-anisoylated streptokinase-plasminogen complex (BRL 26921). Thron Res 1981; 24: 347-87.
    PubMedGoogle Scholar
  • 81 Fears R, Green J, Smith R A G, Walker P. Induction of a sustained fibrinolytic response by BRL 26921 in vitro. Thromb Res 1985; 38: 251-60.
    CrossrefPubMedGoogle Scholar
  • 82 Dupe R J, English P D, Smith R A G, Green J. Acyl-enzymes as thrombolytic agents in dog models of venous thrombosis and pulmonary embolism. Thromb Haemostas 1984; 51: 248-53.
    PubMedGoogle Scholar
  • 83 Marder V J, Rothbard R L, Fitzpatrick P G, Francis C W. Rapid lysis of coronary thrombi with anisoylated plasminogen: streptokinase activator complex. Ann Int Med 1986; 104: 304-10.
    CrossrefPubMedGoogle Scholar
  • 84 Walker I D, Davidson J F, Rae A P, Hutton I, Lawrie T D V. Acyl-streptokinase-plasminogen activator complex in acute myocardial infarction (AMI). Br J Haematol 1983; 53: 344.
    PubMedGoogle Scholar
  • 85 Kasper W, Rückei A, Drexler M, Schenk J. Intracoronary thrombolysis with a new acylated streptokinase-plasminogen activator complex. J Am Coll Cardiol 1983; 01: 615.
    PubMedGoogle Scholar
  • 86 Autrey A. Intracoronary thrombolysis in acute myocardial infarction by means of an acylated derivative of streptokinase plasminogen activator (BRL 26921). Haemostasis 1984; 14: 54.
    PubMedGoogle Scholar
  • 87 Jones C R, Hillis W S, Campbell B C, Fulton W F M. Coronary reperfusion following thrombolytic therapy using BRL 26921. Haemostasis 1984; 14: 55.
    PubMedGoogle Scholar
  • 88 Kasper W, Meinertz T. Fibrinolytic efficacy of a new acylated streptokinase-plasminogen activator complex (BRL 26921) in patients with acute myocardial infarction: comparison between intravenous and intracoronary administration. Thromb Haemostas 1985; 54: 213.
    PubMedGoogle Scholar
  • 89 Doenecke P, Hellstern P, Schwerdt H, Köhler M, Bette L, Wenzel E. Clinical efficacy of acylated streptokinase-plasminogen-complex (BRL 26921) in patients with acute myocardial infarction (AMI). Thromb Haemostas 1985; 54: 271.
    PubMedGoogle Scholar
  • 90 Hillis W S, Hornung R S, Hogg K J, Hockings N, Dunn F G. Successfull early and sustained coronary artery reperfusion using BRL 26921. Thromb Haemostas 1985; 54: 165.
    PubMedGoogle Scholar
  • 91 Bonnier J J RM. Comparison of BRL 26921 (BRL) intravenous (i. v.) with streptokinase (Str.) intracoronary (i.e.) in patients with acute myocardial infarction (A. M. I.). Thromb Haemostas 1985; 54: 165.
    PubMedGoogle Scholar
  • 92 Been M, Boulton F E, De Bono D P. Clinical and haematological effects of intravenous anisoylated plasminogen streptokinase complex. Thromb Haemostas 1985; 54: 212.
    PubMedGoogle Scholar
  • 93 Duckert F, Lämmle B, Marbet G A, Noll G, Lohri A, Huber P, Biland L, Widmer L K, Ritz R, Schmitt H E. Thrombolysis with acylated enzymes in deep vein thrombosis. Haemostasis 1984; 14: 53.
    PubMedGoogle Scholar
  • 94 Kakkar V V, Murray W J G, Lamb J, Scully M F. Acylated streptokinase-plasminogen activator complex and thrombolysis. Haemostasis 1984; 14: 54.
    PubMedGoogle Scholar
  • 95 Trübestein G, Schatz J, Ludwig M, Müller N. Experience with the streptokinase-plasminogen-activator BRL 28921 in the treatment of deep vein thrombosis. Haemostasis 1984; 14: 88.
    PubMedGoogle Scholar
  • 96 Trübestein G, Trübestein R, Ludwig M, Harder T h, Popov S. Streptokinase-plasminogen-complex BRL 26921 and BRL 33575 in deep vein thrombosis. Thromb Haemostas 1985; 54: 272.
    PubMedGoogle Scholar
  • 97 Ausobski J R, Monson J R T, Crow M J, Gilks L, Latif A B, Kester R C, Cruikshank J, Rajah S M. Lysis of acute peripheral arterial thrombus with a new thrombolysis BRL 26921. Thromb Haemostas 1985; 54: 271.
    PubMedGoogle Scholar
  • 98 Collen D. Fibrin specific lysis with tissue type plasminogen activator and single-chain urokinase-type plasminogen activator. Präsentation im Rahmen des »6th International Symposium on Intensive Care and Emergency Medicine«, Brüssel. 1986
    PubMedGoogle Scholar