Abstract
The ability of the organism to liquefy deposited fibrin is a phenomenon that has been known for more than a century (Denis, 1838; Dastre, 1893). Early investigations on this process led to the conclusion that the organism possesses a special system, the function of which is the removal of the end product of blood coagulation, fibrin, after having fulfilled its physiologic function (Denys and De Marbaix, 1889; Delezenne and Pozerski, 1903; Nolf, 1908; Schmitz, 1937). This fibrinolytic system which is specifically adapted to the fragmentation of the insoluble fibrin into soluble split products has been investigated very intensively in the past 30 years. In these studies, its underlying biochemic mechanism, physiologic role, and significance as a pathogenetic principle in certain hemorrhagic disorders became much clearer. This review summarizes some important data of the biochemistry of the factors of the fibrinolytic system and of the mechanisms of their interaction and cooperative action, in order to provide a basis for the understanding of the effects of fibrinolytic and antifibrinolytic therapeutic agents. Detailed descriptions of the fibrinolytic process and its biochemistry were also given by other authors (Astrup, 1956, 1959, 1967; Sherry et al., 1959; Ablondi and Hagan, 1960; MacFarlane, 1964; Fearnley, 1965; Sherry, 1965, 1968; Schwick, 1967; Konttinen, 1968; Robbins and Summaria, 1970, 1971; Bang, 1971; Marder and Sherry, 1972; Astrup and Thorsen, 1972).
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Abiko, Y., Iwamoto, M., Shimizu, M.: Plasminogen-plasmin system. II. Purification and properties of human plasmin. J. Biochem. (Tokyo) 64, 751 (1968)
Abiko, Y., Iwamoto, M., Tomikawa, M.: Plasminogen-plasmin system. V. A stoichiometric equilibrium complex of plasminogen and synthetic inhibitor. Biochim. biophys. Acta (Amst.) 185, 424 (1969)
Ablondi, F., Hagan, J. J.: Plasmin. In: The Enzymes, Vol. IV, New York-London: Academic Press 1960
Ablondi, F., Hagan, J. J., Philips, M., de Renzo, E. G: Inhibition of plasmin, trypsin and the streptokinase-activated fibrinolytic system by ε-aminocaproic acid. Arch. Biochem. 82, 153 (1959)
Albrechtsen, O. K.: The fibrinolytic activity of human tissues. Brit. J. Haemat. 3, 284 (1957a)
Albrechtsen, O. K.: The fibrinolytic activity of human tissues. Acta physiol. scand. 39, 284 (1957b)
Albrechtsen, O. K.: Fibrinolytic activity in the organism. Acta physiol. scand. 47, Suppl. 165, 40 (1959)
Albrechtsen, O. K., Thaysen, J. H.: Fibrinolytic activity in human saliva. Acta physiol. scand. 35, 138(1955)
Ali, S. Y.: Tissue activator of plasminogen (cytokinase). In: Methods in enzymology, Vol. XIX: Proteolytic enzymes. New York-London: Academic Press 1970
Ali, S. Y., Evans, L.: Purification of rabbit kidney cytokinase and a comparison of its properties with human urokinase. Biochem. J. 107, 293 (1968)
Ali, S. Y., Lack, C. H.: Studies on the tissue activator of plasminogen. Distribution of activator and proteolytic activity in the subcellular fractions of rabbit kidney. Biochem. J. 96, 63 (1965)
Alkjaersig, N.: The purification and properties of human plasminogen. Biochem. J. 93, 171 (1964)
Alkjaersig, N., Fletcher, A. P., Sherry, S.: The activation of human plasminogen. I. Spontaneous activation in glycerol. J. biol. Chem. 233, 81 (1958a)
Alkjaersig, N., Fletcher, A. P., Sherry, S.: The activation of human plasminogen. II. A kinetic study of activation with trypsin, urokinase, and streptokinase. J. biol. Chem. 233, 86 (1958b)
Ambrus, C. M., Ambrus, J. L., Roholt, O. A., Meyer, B. K., Shields, R. R.: Insolubilized activators of the fibrinolysin system. In vitro studies. J. Med. 3, 270 (1972)
Ambrus, C. M., Markus, G.: Plasmin-antiplasmin complex as a reservoir of fibrinolytic enzymes. Amer. J. Physiol. 199, 491 (1960)
Andreenko, G. V., Migalina, L. A.: Procedure for isolation and investigation of the characteristics of the tissue activator of plasminogen (Profibrinolysin). Biokhimiya 36, 685 (1971)
Aoki, N., Kaulla, K. N. von: Dissimilarity of human vascular plasminogen activator and human urokinase. J. Lab. clin. Med. 78, 354 (1971)
Aoyagi, T., Miyata, S., Nanbo, M., Kojima, F., Matsuzaki, M., Ishizuka, M., Takeuchi, T., Umezawa, H.: Biological activities of leupeptins. J. Antibiot. (Tokyo) 22, 558 (1969)
Aoyagi, T., Takeuchi, T., Matsuzaki, A., Kawamura, K., Kondo, S., Hamada, M., Maeda, K., Umezawa, H.: Leupeptins, new protease inhibitors from actinomycetes. J. Antibiot. (Tokyo) 22, 283 (1969)
Astrup, T.: Fibrinokinase. Acta physiol. scand. 24, 267 (1951)
Astrup, T.: Fibrinolysis in the organism. Blood 11, 781 (1956)
Astrup, T.: Die Bedeutung der Fibrinolyse. Med. Grundlagenforsch. 2, 197 (1959)
Astrup, T.: Tissue activators of plasminogen. Fed. Proc. 25, 42 (1966)
Astrup, T.: Biologie des Plasmins. Thrombos. Diathes. haemorrh. (Stuttg.) Suppl. 22, 5 (1967)
Astrup, T., Albrechtsen, O. K.: Estimation of the plasminogen activator and the trypsin inhibitor in animal and human tissue. Scand. J. clin. Lab. Invest. 9, 233 (1957)
Astrup, T., Glas, P., Kok, P.: Assay of the plasminogen activator in tissues. In: Thrombosis and bleeding disorders. Theory and Methods. New York: Academic Press 1971
Astrup, T., Kok, P.: Preparation and purification of a plasminogen activator from porcine tissue. Thrombos. Diathes. haemorrh. (Stuttg.) 13, 587 (1965)
Astrup, T., Kok, P.: Assay and preparation of a tissue activator. In: Methods in enzymology, Vol. XIX: Proteolytic enzymes. New York-London: Academic Press 1970
Astrup, T., Permin, P. M.: Fibrinolysis in the animal organism. Nature (Lond.) 159, 681 (1947)
Astrup, T., Rosa, A. T.: A plasminogen proactivator-activator system in human blood effective in absence of Hageman factor. Thrombos. Res. 4, 609 (1974)
Astrup, T., Stage, A.: Isolation of a soluble fibrinolytic activator from animal tissue. Nature (Lond.) 170, 929 (1952)
Astrup, T., Sterndorff, I.: A fibrinolytic system in human milk. Proc. Soc. exp. Biol. (N.Y.) 84, 605 (1953)
Astrup, T., Sterndorff, I.: Fibrinolysokinase activity in animal and human tissue. Acta physiol. scand. 37, 40 (1956)
Astrup, T., Thorsen, S.: The physiology of fibrinolysis. Med. Clin. N. Amer. 56, 153 (1972)
Bachmann, F. W., Fletcher, A. P., Alkjaersig, N., Sherry, S.: Partial purification and properties of the plasminogen activator from pig heart. Biochemistry 3, 1578 (1964)
Bachmann, F. W., Sherry, S.: Purification and properties of plasminogen activator from pig heart. Fed. Proc. 22, 562 (1962)
Back, N., Hiramoto, R., Ambrus, J. L.: Immunohistochemical study of thrombolytic mechanism. Blood 25, 1028 (1965)
Ball, A. P., Silver, D., Day, E. D.: Plasminogen-fibrinogen complex formation as a prelude to fibri-nogenolysis. Density-gradient ultracentrifugation study of radioiodinated systems involving urokinase, plasminogen, and fibrinogen. Thrombos. Diathes. haemorrh. (Stuttg.) 25, 114 (1971)
Bang, N. U.: Physiology and biochemistry of fibrinolysis. In: Thrombosis and Bleeding Disorders, p. 292. New York: Academic Press 1971
Barg, W. F., Boggiano, E., de Renzo, E. C.: Interaction of streptokinase and human plasminogen. II. Starch gel electrophoretic demonstration of a reaction product with activator activity. J. biol. Chem. 240, 2944 (1965)
Barlow, G. H., Lazer, L. V.: Characterization of the plasminogen activator isolated from human embryo kidney cells. Comparison with urokinase. Thrombos. Res. 1, 201 (1972)
Barlow, G. H., Summaria, L., Robbins, K. C.: Molecular weight studies on human plasminogen and plasmin at the microgram level. J. biol. Chem. 244, 1138 (1969)
Barnhart, M. I., Riddle, J. M.: Cellular localization of Profibrinolysin (plasminogen). Blood 21, 306 (1963)
Baumgarten, W., Cole, R. B.: Human plasminogen-streptokinase complex: The question of the existence of a separate activator entity. Thrombos. Diathes. haemorrh. (Stuttg.) 5, 605 (1961)
Beard, E. L., Busuttil, R. W., Gottshalk, S. K.: Stress induced release of plasminogen activator from lysosomes. Thrombos. Diathes. haemorrh. (Stuttg.) 21, 20 (1969)
Beard, E. L., Montuori, M. H., Danos, G. J.: Plasminogen activator activity of rat lysosomes. Proc. Soc. exp. Biol. (N. Y.) 129, 804 (1968)
Berg, W.: Urokinase activation of plasminogen and spontaneous inactivation of the plasmin formed. A kinetic study. Thrombos. Diathes. haemorrh. (Stuttg.) 19, 145 (1968)
Bernik, M. B.: Increased plasminogen activator (urokinase) in tissue culture after fibrin deposition. J. clin. Invest. 52, 823 (1973)
Bernik, M. B., Kwaan, H. C.: Origin of fibrinolytic activity in cultures of the human kidney. J. Lab. clin. Med. 70, 650 (1967)
Bernik, M. B., Kwaan, H. C.: Plasminogen activator activity in cultures from human tissues. An immunological and histochemical study. J. clin. Invest. 48, 1740 (1969)
Bernik, M. B., White, W. F., Oller, E. P., Kwaan, H. C.: Immunologic identity of plasminogen activator in human urine, heart, blood vessels, and tissue culture. J. Lab. clin. Med. 84, 546 (1974)
Bickford, A. F., Taylor, F. B., Sheena, R.: Inhibition of the fibrinogen-plasmin reaction by ω-aminocarboxylic acids and alkylamines. Biochim. biophys. Acta (Amst.) 92, 328 (1964)
Bilinski, T., Loch, T., Zakrzewski, K.: Studies on streptokinase. Purification and some molecular properties. Acta biochim. pol. 15, 123 (1968)
Birktoft, J. J., Blow, D. M., Henderson, R., Steitz, T. A.: The structure of α-chymotrypsin. Phil. Trans. B 257, 67 (1970)
Blatt, W. F., Segal, H., Gray, J. L.: Purification of streptokinase and human plasmin and their interaction. Thrombos. Diathes. haemorrh. (Stuttg.) 11, 393 (1964)
Blombäck, B., Blombäck, M.: Purification of human and bovine fibrinogen. Ark. Kemi 10, 415 (1957)
Blombäck, B., Blombäck, M., Hessel, B., Iwanaga, S.: Structure of N-terminal fragments of fibrinogen and specificity of thrombin. Nature (Lond.) 215, 1445 (1967)
Brockway, W. J., Castellino, F. J.: The mechanism of the inhibition of plasmin activity by ε-aminocaproic acid. J. biol. Chem. 246, 4641 (1971)
Brockway, W. J., Castellino, F. J.: Measurement of the binding of antifibrinolytic amino acids to various plasminogens. Arch. Biochem. 151, 194 (1972)
Brockway, W. J., Castellino, F. J.: A characterization of native streptokinase and altered streptokinase isolated from a human plasminogen activator complex. Biochemistry 13, 1063 (1974)
Bruner-Lorand, J., Pilkington, T. R. E., Lorand, L.: Inhibitors of fibrin cross-linking: relevance for thrombolysis. Nature (Lond.) 210, 1273 (1966)
Buck, F. F., Boggiano, E.: Interaction of streptokinase and human plasminogen. VI. Function of the streptokinase moiety in the activator complex. J. biol. Chem. 246, 2091 (1971)
Buck, F. F., Hummel, B. C. W., de Renzo, E. C.: Interaction of streptokinase and human plasminogen. V. Studies on the nature and mechanism of formation of the enzymatic site of the activator complex. J. biol. Chem. 243, 3648 (1968)
Buck, F. F., de Renzo, F. C.: Naphthyl-acetate-esterase activity of streptokinase preparations. Biochim. biophys. Acta (Amst.) 89, 348 (1964)
Burges, R. A., Brammer, K. W., Coombes, J. D.: Molecular weight of urokinase. Nature (Lond.) 208, 894 (1965)
Capet-Antonini, F. C., Grimard, M., Tamenasse, J.: Properties of two types of solid-phase urokinase preparations. Thrombos. Res. 2, 479 (1973)
Cartwright, T.: Partial purification of a specific plasminogen activator from porcine parotid glands. Thrombos. Diathes. haemorrh. (Stuttg.) 31, 403 (1974)
Castellino, F. J., Brockway, W. J., Thomas, J. K., Liao, H., Rawitch, A. B.: Rotational diffusion analysis of the conformational alterations produced in plasminogen by certain antifibrinoly-tic amino acids. Biochemistry 12, 2787 (1973a)
Castellino, F. J., Siefring, G. E., Sodetz, J. M., Bretthauer, R. K.: Amino terminal amino acid sequences and carbohydrate of the two major forms of rabbit plasminogen. Biochem. Biophys. Res. Commun. 53, 845 (1973b)
Celander, D. R., Guest, M. M.: The biochemistry and physiology of urokinase. Amer. J. Cardiol. 6, 409 (1960)
Celander, D. R., Langlinais, R. P., Guest, M. M.: The application of foam technique to the partial purification of an urine activator of plasma Profibrinolysin. Arch. Biochem. 55, 286 (1955)
Chan, J. Y. S., Mertz, E. T.: Studies on plasminogen. IV. Alteration of bovine and human plasminogens during isolation. Canad. J. Biochem. 44, 469 (1966a)
Chan, J. Y. S., Mertz, E. T.: Studies on plasminogen. V. Purification of bovine and human plasminogens by Sephadex chromatography. Canad. J. Biochem. 44, 475 (1966b)
Chan, J. Y. S., Mertz, E. T.: Studies on plasminogen. VI. Activation products of bovine and human plasminogens. Canad. J. Biochem. 44, 487 (1966c)
Chase, T., Shaw, E.: Comparison of the esterase activities of trypsin, plasmin, and thrombin on guanidinobenzoate esters. Titration of the enzymes. Biochemistry 8, 2212 (1969)
Chen, R., Doolittle, R. F.: γ-γ-Cross-linking sites in human and bovine fibrin. Biochemistry 10, 4486 (1971)
Chesterman, C. N., Allington, M. J., Sharp, A. A.: Relation of plasminogen activator to fibrin. Nature (Lond.) 238, 15 (1972)
Chesterman, C. N., Cederholm-Williams, S. A., Allington, M. J., Sharp, A. A.: The degradation of streptokinase during the production of plasminogen activator. Thrombos. Res. 5, 413 (1974)
Christensen, L. R.: Streptococcal fibrinolysis: a proteolytic reaction due to a serum enzyme activated by streptococcal fibrinolysin. J. gen. Physiol. 28, 363 (1945)
Christensen, L. R.: Methods for measuring the activity of components of the streptococcal fibrinolytic system, and streptococcal desoxyribonuclease. J. clin. Invest. 28, 163 (1949)
Christensen, L. R., McLeod, C. M.: A proteolytic enzyme of serum: characterization, activation and reaction with inhibitors. J. gen. Physiol. 28, 559 (1945)
Christensen, L. R., Smith, D. H.: Plasminogen purification by acid extraction. Proc. Soc. exp. Biol. (N.Y.) 74, 840 (1950)
Christman, J. K., Acs, G.: Purification and characterization of a cellular fibrinolytic factor associated with oncogenic transformation : The plasminogen activator from SV-40-transformed hamster cells. Biochim. biophys. Acta (Amst.) 340, 339 (1974)
Claeys, H., Amery, A., Verhaege, R.: Proteolytic activity of the activator produced by streptokinase in human plasma. Thrombos. Diathes. haemorrh. (Stuttg.) 26, 88 (1971)
Claeys, H., Molla, A., Verstraete, M.: Conversion of the NH2-terminal glutamic acid to NH2-terminal lysine human plasminogen by plasmin. Thrombos. Res. 3, 515 (1973)
Clayes, H., Vermylen, J.: Physico-chemical and proenzyme properties of NH2-terminal glutamic acid and NH2-terminal lysine human plasminogen. Biochim. biophys. Acta (Amst.) 342, 351 (1974)
Cliffton, E. E., Cannamela, D. A.: Proteolytic and fibrinolytic activity of serum. Activation by streptokinase and staphylokinase indicating dissimilarities of enzymes. Blood 8, 554 (1953)
Coats, E. A.: Comparative inhibition of thrombin, plasmin, trypsin, and complement by benzamidines using substituent constants and regression analysis. J. med. Chem. 16, 1102 (1973)
Cole, E. R.: Hydrolysis of l-histidine methyl ester. II. Activity of various proteolytic enzymes with special reference to activators of plasminogen. Thrombos. Diathes. haemorrh. (Stuttg.) 19, 334(1968)
Cole, E. R., Olwin, J. H.: Hydrolysis of l-histidine methyl ester by proteolytic enzymes with particular reference to thrombin and plasminogen activators. Thrombos. Diathes. haemorrh. (Stuttg.) 18, 304 (1967)
Colgan, J., Gates, E., Miller, L. L.: Serum and urinary fibrinolytic activity related to the hemorrhagic diathesis in irradiated dogs. J. exp. Med. 95, 531 (1952)
Collen, D., de Mayer, L.: Molecular biology of human plasminogen. I. Physicochemical properties and microheterogeneity. Thrombos. Diathes. haemorrh. (Stuttg.) 34, 396 (1975)
Collen, D., Verstraete, M.: Molecular biology of human plasminogen II. Metabolism in physiological and some pathological conditions in man. Thrombos. Diathes. haemorrh. (Stuttg.) 34, 403 (1975)
Colman, R. W.: Activation of plasminogen by human plasma kallikrein. Biochem. biophys. Res. Commun. 35, 273 (1969)
Coughlin, W. R.: Circulating plasminogen activator. Ph. D. Thesis, Yale University, 1966
Dastre, A.: Fibrinolyse dans le sang. Arch. physiol. (Paris) 5, 661 (1893)
Davidson, F. M.: The activation of plasminogen by staphylokinase : Comparison with streptokinase. Biochem. J. 76, 56 (1960a)
Davidson, F. M.: Activation of plasminogen by staphylokinase. Nature (Lond.) 185, 626 (1960b)
Davies, M. C., Englert, M. E.: Physical properties of highly purified human plasminogen. J. biol. Chem. 235, 1011 (1960)
Davies, M. C., Englert, M. E., de Renzo, E. C.: Interaction of streptokinase and human plasminogen. I. Combining of streptokinase and plasminogen observed in the ultracentrifuge under a variety of experimental conditions. J. biol. Chem. 239, 2651 (1964)
Delezenne, C., Pozerski, E.: Action du sèrum sanguin sur la gélatine, en présence du chloroforme. C. R. Soc. Biol. (Paris) 55, 327 (1903)
Denis, P. S.: Essai sur l’Application de la Chimie à l’Etude Physiologique du Sang de l’Homme, et à l’Etude Physiologique, Hygienique et Thérapeutique des Maladies de Cette Humeur. Paris: Bechet, Jr. 1838
Denys, J., de Marbaix, H.: Les peptonisations provoqués par le chloroforme. Cellule 5, 197 (1889)
Derechin, M.: Purification of human plasminogen. Biochem. J. 82, 241 (1962)
Derechin, M., Johnson, P., Szuchet, S.: Further studies with human plasminogen. Biochem. J. 84, 336 (1962)
Deutsch, E., Eisner, P.: The mechanism of fibrinolysis induced by bacterial pyrogens. Thrombos. Diathes. haemorrh. (Stuttg.) 3, 286 (1959)
Deutsch, D. G., Mertz, E. T.: Plasminogen: purification from human plasma by affinity chromatography. Science 170, 1095 (1970)
Deutsch, D. G., Mertz, E. T.: Activation of plasminogen with insoluble derivatives of urokinase. J. Med. (Basel) 3, 224 (1972)
Dillon, H. C., Jr., Wannamaker, L. W.: Physical and immunological differences among streptokinases. J. exp. Med. 121, 351 (1965)
Doleschel, W.: Isolierung einer dritten humanen Urokinase (S0-Typ). Wien. klin. Wschr. 87, 282 (1975)
Doleschel, W., Auerswald, W.: Determination of molecular weights of uroprotein fraction with urokinase activity by means of molecular sieving. Med. Pharmacol. exp. (Basel) 16, 225 (1967)
Duckert, F.: Urokinase. In: Current problems in clinical biochemistry. II: Enzymes in urine and kidney. Bern-Stuttgart: Huber 1968
Engel, A., Alexander, B., Pechet, L.: Activation of trypsinogen and plasminogen by thrombin preparations. Biochemistry 5, 1543 (1966)
Epstein, M. D., Beller, F. K., Douglas, G. W.: Kidney tissue activator of fibrinolyses in relation to pregnancy. Obstet. Gynec. 32, 494 (1968)
Fearnley, G. R.: Fibrinolysis. London: Edward Arnold Publishers 1965
Fearnley, G. R., Ferguson, J.: Arteriovenous differences in natural fibrinolysis. Lancet 1957 II, 1040
Fearnley, G. R., Tweed, J. M.: An active fibrinolytic enzyme in plasma of normal people with observations on inhibition associated with the presence of calcium. Clin. Sci. 12, 81 (1953)
Feddersen, C., Gormsen, J.: Plasmin digestion of stabilized and nonstabilized fibrin illustrated by immunoelectrophoresis and hemagglutination inhibition immunoassays. Scand. J. Haematol. 8,461 (1971a)
Feddersen, C., Gormsen, J.: Plasmin digestion of stabilized and nonstabilized fibrin illustrated by pH-stat titration and thrombelastography. Scand. J. clin. Lab. Invest. 27, 195 (1971b)
Fletcher, A. P., Alkjaersig, N., Sherry, S.: The maintenance of a sustained thrombolytic state in man. I. Induction and effects. J. clin. Invest. 38, 1096 (1959)
Fletcher, A. P., Alkjaersig, N., Sherry, S.: Pathogenesis of the coagulation defect developing during pathological plasma proteolytic (“fibrinolytic”) states. I. The significance of fibrinogen proteolysis and circulating fibrinogen breakdown products. J. clin. Invest. 41, 896 (1962)
Fletcher, A. P., Alkjaersig, N., Sherry, S., Genton, E., Hirsh, J., Bachmann, F.: The development of urokinase as a thrombolytic agent. Maintenance of a sustained thrombolytic state in man by its intravenous infusion. J. Lab. clin. Med. 65, 713 (1965)
Gaffney, P. J., Brasher, M.: Subunit structure of the plasmin-induced degradation products of crosslinked fibrin. Biochim. biophys. Acta (Amst.) 295, 308 (1973)
Gajewski, J., Markus, G.: A new method for plasminogen standardization. Thrombos. Diathes. haemorrh. (Stuttg.) 20, 548 (1968)
Geratz, J. D.: Inhibition of thrombin, plasmin and plasminogen activation by amidino compounds. Thrombos. Diathes. haemorrh. (Stuttg.) 23, 486 (1970)
Geratz, J. D.: Inhibition of coagulation and fibrinolysis by aromatic amidino compounds. Thrombos. Diathes. haemorrh. (Stuttg.) 25, 391 (1971)
Geratz, J. D.: Kinetic aspects of the irreversible inhibition of trypsin and related enzymes by p-[m-(-m-fluorosulfonylphenylureido)-phenoxyethoxy]-benzamidine. FEBS-Letters 20, 294 (1972)
Geratz, J. D.: Structure-activity relationships for the inhibition of plasmin and plasminogen activation by aromatic diamidines and a study of the effect of plasma proteins on the inhibition process. Thrombos. Diathes. haemorrh. (Stuttg.) 29, 154 (1973)
Geratz, J. D., Cheng, M. C.-F.: The inhibition of urokinase by aromatic diamidines. Thrombos. Diathes. haemorrh. (Stuttg.) 33, 230 (1975)
Glas, P., Astrup, T.: Thromboplastin and plasminogen activator in tissues of the rabbit. Amer. J. Physiol. 219, 1140 (1970)
Gormsen, J., Feddersen, C.: Degradation of stabilized and nonstabilized fibrin clots by plasmin. Immunological study. Ann. N. Y. Acad. Sci. 202, 329 (1972)
Gormsen, J., Fletcher, A. P., Alkjaersig, N., Sherry, S.: Enzymic lysis of plasma clots: The influence of fibrin stabilization on lysis rates. Arch. Biochem. 120, 654 (1967)
Groskopf, W. R., Hsieh, B., Summaria, L., Robbins, K. C.: The specificity of human plasmin on the B-chain of oxidized bovine insulin. Biochim. biophys. Acta (Amst.) 168, 376 (1968)
Groskopf, W. R., Hsieh, B., Summaria, L., Robbins, K. C.: Studies on the active center of human plasmin. The serine and histidine residue. J. biol. Chem. 244, 359 (1969a)
Groskopf, W. R., Summaria, L., Robbins, K. C.: Studies on the active center of human plasmin. Partial amino acid sequence of a peptide containing the active center serine residue. J. biol. Chem. 244, 3590 (1969b)
Guest, M. M., Celander, D. R.: Urokinase: physiologic activator of Profibrinolysin. Tex. Rep. Biol. Med. 19, 89 (1961)
Gutmann, M., Rimon, A.: Studies on the activator of plasminogen. II. The nature of the proactivator. Canad. J. Biochem. 42, 1339 (1964)
Hagan, J. J., Ablondi, F. B., de Renzo, E. C.: Purification and biochemical properties of human plasminogen. J. biol. Chem. 235, 1005 (1960)
Hartley, B. S.: Amino-acid sequence of bovine chymotrypsinogen A. Nature (Lond.) 201, 1284 (1964)
Hartley, B. S.: Homologies in serine proteinases. Phil. Trans. B 257, 77 (1970)
Hayes, M. L., Brethauer, R. K., Castellino, F. J.: Carbohydrate compositions of the rabbit plasminogen isoenzymes. Arch. Biochem. 171, 651 (1975)
Heberlein, P. J., Barnhart, M. I.: Canine plasminogen: Purification and demonstration of multi-molecular forms. Biochim. biophys. Acta (Amst.) 168, 195 (1968)
Heimburger, N.: Neuere Erkenntnisse über den Mechanismus der Fibrinolyse unter besonderer Berücksichtigung der Fibrinagar-Elektrophorese. Behringwerk-Mitt. Heft 41, 84 (1962)
Heimburger, N.: Basis mechanism of action of Streptokinase and urokinase. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 47, 21 (1971)
Heimburger, N., Schwick, H. G.: Beitrag zur Charakterisierung des durch Streptokinase induzierten Aktivators. Arzneimittel-Forsch. 21, 1439 (1971)
Henderson, K. W., Nußbaum, M.: Mechanism of enhanced streptokinase-induced clot lysis following in vitro Factor-XIII inactivation. Brit. J. Haemat. 17, 445 (1969)
Henderson, R.: Structure of crystalline α-chymotrypsin. IV. The structure of indoleacryloyl-α-chymotrypsin and its relevance to the hydrolytic mechanism of the enzyme. J. molec. Biol. 54, 341 (1970)
Henderson, R., Wright, C. S., Hess, G. P., Blow, D. M.: α-Chymotrypsin: What can we learn about catalysis from X-ray diffraction. Cold Spr. Harb. Symp. quant. Biol. 36, 63 (1971)
Hijikata, A., Fujimoto, K., Kitaguchie, H., Okamoto, S.: Some properties of the tissue plasminogen activator from the pig heart. Thrombos. Res. 4, 731 (1974)
Höpfinger, L. M., Mertz, E. T.: Studies on plasminogen. VII. Mechanism of activation of bovine plasminogen. Canad. J. Biochem. 47, 909 (1969)
Hummel, B. C. W., Buck, F. F., de Renzo, E. C.: Interaction of streptokinase and human plasminogen. III. Plasmin and activator activities in reaction mixtures of streptokinase and human plasminogen or human plasmin of various molar ratios. J. biol. Chem. 241, 347 (1966)
Iwamoto, M., Abiko, Y., Shimizu, M.: Plasminogen-plasmin system. III. Kinetics of plasminogen activation and inhibition of plasminogen-plasmin system by some synthetic inhibitors. J. Biochem. (Tokyo) 64, 759 (1968)
Iwanaga, S., Wallén, P., Gröndahl, N. J., Henschen, A., Blombäck, B.: Isolation and characterization of N-terminal fragments obtained by plasmin digestion of human fibrinogen. Biochim. biophys. Acta (Amst.) 147, 606 (1967)
Jackson, H. D., Mertz, E. T.: Activation of bovine plasminogen by trypsin. Proc. Soc. exp. Biol. (N.Y.) 86, 827 (1954)
Jacobsson, K.: Activation of plasminogen with trypsin. Acta chem. scand. 7, 430 (1953)
Johnson, A. J., Kline, D. L., Alkjaersig, N.: Assay methods and standard preparations for plasmin, plasminogen and urokinase in purified systems 1967–1968. Thrombos. Diathes. haemorrh. (Stuttg.) 21, 259 (1969)
Kaulla, K. N. von: Urine adsorbate with fibrinolytic and thromboplastic properties. J. Lab. clin. Med. 44, 944 (1954)
Kaulla, K. N. von: Methods for preparation of purified human thromboplastin and fibrinolysokinase from urine. Acta haematol. (Basel) 16, 315 (1956a)
Kaulla, K. N. von: Extraction and concentration of thromboplastic material from human urine. Proc. Soc. exp. Biol. (N. Y.) 91, 543 (1956b)
Kaulla, K. N. von, Shettles, L. B.: Relationship between human seminal fluid and the fibrinolytic system. Proc. Soc. exp. Biol. (N. Y.) 83, 692 (1953)
Kaulla, K. N. von, Swan, H.: Clotting deviations in man during cardiac bypass; fibrinolysis and circulating anticoagulant. J. thorac. Cardiovasc. Surg. 36, 519 (1958)
Kawano, T., Morimoto, K., Uemura, Y.: Urokinase inhibitor in human placenta. Nature (Lond.) 217, 253 (1968)
Kawano, T., Morimoto, K., Uemura, Y.: Partial purification and properties of urokinase inhibitor from human placenta. J. Biochem. (Tokyo) 67, 333 (1970)
Kawano, T., Uemura, Y.: Inhibition of tissue activator by urokinase inhibitor. Thrombos. Diathes. haemorrh. (Stuttg.) 25, 129 (1971)
Kickhöfen, G., Struwe, F. E., Bramesfeld, B., Westphal, O.: Über einige Beobachtungen am Uropepsinogen und Plasminogen-Aktivator des menschlichen Urins. Biochem. Z. 330, 467 (1958)
Kjeldgaard, N. O., Ploug, J.: Urokinase an activator of plasminogen from human urine. II. Mechanism of plasminogen activation. Biochim. biophys. Acta (Amst.) 24, 283 (1957)
Kline, D. L.: The purification and crystallization of plasminogen (Profibrinolysin). J. biol. Chem. 204, 904 (1953)
Kline, D. L.: Caseinolytic techniques. In: Thrombosis and Bleeding Disorders. New York-London: Academic Press 1971
Kline, D. L., Fishman, J. B.: Improved procedure for the isolation of human plasminogen. J. biol. Chem. 236, 3232 (1961a)
Kline, D. L., Fihsman, J. B.: Proactivator function of human plasmin as shown by lysine esterase assay. J. biol. Chem. 236, 2807 (1961b)
Kline, D. L., Ts’ao, C.-H.: The direct activation of human plasminogen by streptokinase. Thrombos. Diathes. haemorrh. (Stuttg.) 18, 288 (1967)
Kline, D. L., Ts’ao, C.-H.: Activation of human plasminogen by streptokinase in absence of plasmin-SK activator. Amer. J. physiol. 220, 440 (1971)
Kok, P., Astrup, T.: Some comparative studies on tissue activator and urokinase. Thrombos. Diathes. haemorrh. (Stuttg.) 18, 294 (1967)
Kok, P., Astrup, T.: Isolation and purification of a tissue activator and its comparison with urokinase. Biochemistry 8, 79 (1969)
Konttinen, Y. P.: Fibrinolysis. Chemistry, physiology, pathology and clinics. Tampere: Star 1968
Kopitar, M., Stegnar, M., Accetto, B., Lebez, D.: Isolation and characterization of plasminogen activator from pig leukocytes. Thrombos. Diathes. haemorrh. (Stuttg.) 31, 72 (1974)
Kosow, D. P.: Kinetic mechanism of the activation of human plasminogen by streptokinase. Biochemistry 14, 4459 (1975)
Kowalski, E., Kopeć, M., Latallo, Z., Rozkowski, S., Sendys, N.: On the occurrence of a plasminogen-like substance in human tissues. Blood 8, 436 (1958)
Kowalski, E., Latallo, Z., Niewiarowski, S.: Untersuchungen über die Aktivierung des Plasminogens und die Inaktivierung des Plasmins. Folia haemat. (Lpz.) 75, 225 (1957)
Krieger, M., Kay, L. M., Stroud, R. M.: Structure and specific binding of trypsin: Comparison of inhibited derivatives and a model for substrate binding. J. molec. Biol. 83, 209 (1974)
Kucinski, C. S., Fletcher, A. P., Sherry, S.: Effect of urokinase antiserum on plasminogen activators: Demonstration of immunologic dissimilarity between plasma plasminogen activator and urokinase. J. clin. Invest. 47, 1238 (1968)
Kwaan, H. C., Fischer, S.: Localization of fibrinolytic activity in kidney tissues. Fed. Proc. 24, 387 (1965)
Kwaan, H. C., Lai, K. S., McFadzean, A. J. S.: Lysokinase activity in ascitic fluid. Lancet 1960 I, 1327
Laake, K., Venneröd, A. M.: Factor XH-inducedfibrinolysis: Studies on the separation of prekallikrein, plasminogen proactivator, and factor XI in human plasma. Thrombos. Res. 4, 285 (1974)
Lack, C. H., Ali, S. Y.: Tissue activator of plasminogen. Nature (Lond.) 201, 1030 (1964)
Lack, C. H., Glanville, K. L. A.: Staphylokinase. In: Methods in enzymology. XIX: Proteolytic enzymes. New York-London : Academic Press 1970
Ladehoff, A. A.: The content of plasminogen activator in the human urinary tract. Scand. J. clin. Lab. Invest. 12, 136 (1960)
Landmann, H.: Vergleichende Untersuchungen über Antifibrinolytika. Folia haemat. (Lpz.) 87, 106 (1967)
Landmann, H.: Synthetische Hemmstoffe des Plasmins. Haematologia (Budapest), Suppl. 1, 169 (1970)
Landmann, H.: Studies on the mechanism of action of synthetic antifibrinolytics. A comparison with the action of derivatives of benzamidine on the fibrinolytic process. Thrombos. Diathes. haemorrh. (Stuttg.) 29, 253 (1973)
Landmann, H., Markwardt, F.: Irreversible synthetische Inhibitoren der Urokinase. Experientia (Basel) 26, 145 (1970)
Lassen, M.: The esterase activity of the fibrinolytic system. Biochem. J. 69, 360 (1958)
Lassen, M.: Evidence of the different nature of human plasminogen and proactivator. Acta chem. scand. 13, 1064 (1959a)
Lassen, M.: The reaction between streptokinase and human plasma. Acta chem. scand. 13, 1332 (1959b)
Latallo, Z. S., Teisseyre, E.: Preliminary experience with a new chromogenic substrate in studies on blood coagulation and fibrinolysis. 9th FEBS-Meeting, Abstr. f 3 a 6, Budapest 1974
Lauritsen, O. S.: Urokinase inhibitor in human plasma. Scand. J. clin. Lab. Invest. 22, 314 (1968)
Lesuk, A., Terminiello, L., Traver, J. H.: Crystalline human urokinase: Some properties. Science 147, 880(1965)
Lesuk A., Terminiello, L., Traver, J. H., Groff, J. L.: Biochemical and biophysical studies of human urokinase. Thrombos. Diathes. haemorrh. (Stuttg.) 18, 293 (1967a)
Lesuk, A., Terminiello, L., Traver, J. H., Groff, J. L.: Proteolytic degradation of human urokinase to active fragments. Fed. Proc. 26, 647 (1967b)
Lewis, J. H., Ferguson, J. H.: Activation of dog serum Profibrinolysin by staphylokinase. Amer. J. Physiol. 166, 594 (1951)
Lewis, J. H., Ferguson, J. H.: Activation of Profibrinolysin by trypsin. Amer. J. Physiol. 170, 636 (1952)
Ling, C.-M., Summaria, L., Robbins, K. C.: Mechanism of formation of bovine plasminogen activator from human plasmin. J. biol. Chem. 240, 4213 (1965)
Ling, C.-M., Summaria, L., Robbins, K. C.: Isolation and characterization of bovine plasminogen activator from a human plasminogen-streptokinase mixture. J. biol. Chem. 242, 1419 (1967)
Lorand, L., Condit, E. V.: Ester hydrolysis by urokinase. Biochemistry 4, 265 (1965)
Lorand, L., Jacobsen, A.: Accelerated lysis of blood clots. Nature (Lond.) 195, 911 (1962)
Lorand, L., Mozen, M. M.: Ester hydrolyzing activity of urokinase preparations. Nature (Lond.) 201, 392 (1964)
Lorand, L., Nilsson, J. G. L.: Molecular approach for designing inhibitors to enzymes involved in blood clotting. In: Drug Design. III. New York-London : Academic Press 1971
Lundquist, F., Thorsteinson, T., Buus, O.: Purification and properties of some enzymes in human seminal plasma. Biochem. J. 59, 59 (1955)
MacFarlane, R. G.: The development of ideas on fibrinolysis. Brit. med. Bull. 20, 173 (1964)
MacFarlane, R. G., Pilling, J.: Fibrinolytic activity of normal urine. Nature (Lond.) 159, 779 (1947)
Magnusson, S., Sottrup-Jensen, L., Claeys, H., Zajdel, M., Petersen, T. E.: Complete primary structure of prothrombin, partial primary structures of plasminogen and hirudin. 5th Congr. Int. Soc. Thromb. Haemostasis, Abstr. 200, Paris 1975 a
Magnusson, S., Sottrup-Jensen, L., Claeys, H., Zajdel, M., Petersen, T. E.: Extensive sequence homology in the nonserine protease parts of prothrombin and plasminogen. A general structure common to large zymogens? 10th FEBS-Meeting. Abstr. 904, Paris 1975b
Marder, V. J., Sherry, S.: Fibrinolysis. In: Pathophysiology. Philadelphia: J. B. Lippincott 1972
Mares-Guia, M., Shaw, E.: Studies on the active center of trypsin. The binding of amidines and guanidines as models of substrate side chain. J. biol. Chem. 240, 1579 (1965)
Markus, G., Ambrus, C. M.: On the formation of different types of plasmin by streptokinase activation. J. biol. Chem. 235, 1673 (1960)
Markus, G., Werkheiser, W. C.: The interaction of streptokinase with plasminogen. I. Functional properties of the activated enzyme. J. biol. Chem. 239, 2637 (1964)
Markwardt, F., Landmann, H.: Blutgerinnungshemmende Proteine, Peptide und Aminosäurederivate. In: Handbuch der experimentellen Pharmakologie, Vol.XXVII. Berlin-Heidelberg-New York: Springer 1971
Markwardt, F., Landmann, H., Klöcking, H.-P.: Fibrinolytika und Antifibrinolytika. Jena: Fischer 1972a
Markwardt, F., Landmann, H., Walsmann, P.: Comparative studies on the inhibition of trypsin, plasmin, and thrombin by derivatives of benzylamine and benzamidine. Europ. J. Biochem. 6, 502 (1968)
Markwardt, F., Wagner, G., Walsmann, P., Horn, H., Stürzebecher, J.: Inhibition of trypsin and thrombin by amidinophenyl esters of aromatic carboxylic acids. Acta biol. med. germ. 28, K 19 (1972b)
Markwardt, F., Walsmann, P., Landmann, H.: Hemmung der Thrombin-, Plasmin- und Trypsin-wirkung durch Alkyl- und Alkoxybenzamidine. Pharmazie 25, 551 (1970b)
Markwardt, F., Richter, M., Walsmann, P., Landmann, H.: The inhibition of trypsin, plasmin, and thrombin by benzyl 4-guanidino benzoate and 4′-nitrobenzyl 4-guanidinobenzoate. FEBS-Letters 8, 170(1970a)
Markwardt, F., Walsmann, P., Richter, M., Klöcking, H.-P., Drawert, J., Landmann, H.: Aminoal-kylbenzolsulfofluoride als Fermentinhibitoren. Pharmazie 26, 401 (1971)
Markwardt, F., Walsmann, P., Stürzebecher, J., Landmann, H., Wagner, G.: Synthetische Inhibitoren von Serinproteinasen. 1. Mitteilung: Über die Hemmung von Trypsin, Plasmin und Thrombin durch Ester der Amidino- und Guanidinobenzoesäure. Pharmazie 28, 326 (1973)
McCall, D. C., Kline, D. L.: Mechanism of action and some properties of a tissue activator of plasminogen. Thrombos. Diathes. haemorrh. (Stuttg.) 14, 116 (1965)
McClintock, D. K., Bell, P. H.: The mechanism of activation of human plasminogen by streptokinase. Biochem. Biophys. Res. Commun. 43, 694 (1971)
McClintock, D. K., Englert, M. E., Dziobkowski, C., Snedeker, E. H., Bell, P. H.: Two distinct pathways of the streptokinase-mediated activation of highly purified human plasminogen. Biochemistry 13, 5334 (1974)
McConnel, D., Johnston, J. G., Young, I., Holemans, R.: Localization of plasminogen activator in kidney. Lab. Invest. 15, 980 (1966)
McKee, P. A., Lemmon, W. B., Hampton, J. W.: Streptokinase and urokinase activation of human, chimpanzee and baboon plasminogen. Thrombos. Diathes. haemorrh. (Stuttg.) 26, 512 (1971)
Mihara, H., Fujii, T., Okamoto, S.: Fibrinolytic activity of cerebro-spinal fluid and the development of artificial cerebral haematomas in dogs. Thrombos. Diathes. haemorrh. (Stuttg.) 21, 294 (1969)
Milstone, H.: A factor in normal human blood which participates in streptococcal fibrinolysis. J. Immunol. 42, 109 (1941)
Morgan, F. J., Henschen, A.: The structure of streptokinase. I. Cyanogen bromide fragmentation, amino acid composition and partial amino acid sequences. Biochim. biophys. Acta (Amst.) 181, 93 (1969)
Mosesson, W. M.: The preparation of human fibrinogen free of plasminogen. Biochim. biophys. Acta (Amst.) 57, 204 (1962)
Mounter, L. A., Mounter, M. E.: The inhibition of hydrolytic enzymes by organophosphorous compounds. J. biol. Chem. 238, 1079 (1963)
Mounter, L. A., Shipley, B. A.: The inhibition of plasmin by toxic phosphorous compounds. J. biol. Chem. 231, 855 (1958)
Movat, H. Z., Burrowes, C. E., Soltay, M. J., Takeuchi, Y., Habal, F., Özge-Anwar, A. H.: Interrelation between the clotting, fibrinolytic, and kinin systems of human plasma. Protides Biol. Fluids, Proc. Colloq. 20, 315 (1972)
Müllertz, S.: Formation and properties of the activator of plasminogen and of human and bovine plasmin. Biochem. J. 61, 424 (1955)
Müllertz, S.: Mechanism of activation and effect of plasmin in blood. Acta physiol. Scand. 38, Suppl. 130 (1956)
Müllertz, S.: Activation of plasminogen. Ann. N.Y. Acad. Sci. 68, 38 (1957)
Müllertz, S.: Different molecular forms of plasminogen and plasmin produced by urokinase in human plasma and their relation to protease inhibitors and lysis of fibrinogen and fibrin. Biochem. J. 143, 273 (1974)
Muramatu, M., Fujii, S.: Inhibitory effects of ω-guanidino acid esters on trypsin, plasmin, thrombin and plasma kallikrein. J. Biochem. (Tokyo) 64, 807 (1968)
Muramatu, M., Fujii, S.: Inhibitory effects of ω-amino acid esters on the activity of trypsin, plasmin and thrombin. J. Biochem. (Tokyo) 65, 17 (1969)
Muramatu, M., Fujii, S.: Inhibitory effects of ω-amino acid esters on trypsin, plasmin, plasma kallikrein and thrombin. Biochim. biophys. Acta (Amst.) 242, 203 (1971)
Muramatu, M., Fujii, S.: Inhibitory effects of ω-guanidino acid esters on trypsin, plasmin, plasma kallikrein and thrombin. Biochim. biophys. Acta (Amst.) 268, 221 (1972)
Muramatu, M., Hayakumo, Y., Fujii, S.: Synthetic inhibitors of trypsin, plasmin, and chymotrypsin. J. Biochem. (Tokyo) 62, 408 (1967)
Muramatu, M., Hayakumo, Y., Onishi, T., Sato, T., Fujii, S.: Comparison of human plasmin formed by activation with trace and large amounts of streptokinase. J. Biochem. (Tokyo) 65, 329 (1969)
Muramatu, M., Onishi, T., Makino, S., Fujii, S., Yamamura, Y.: Inhibition of caseinolytic activity of plasmin by various synthetic inhibitors. J. Biochem. (Tokyo) 57, 402 (1965a)
Muramatu, M., Onishi, T., Makino, S., Fujii, S., Yamamura, Y.: Inhibition of fibrinolytic activity of plasmin by various synthetic inhibitors. J. Biochem. (Tokyo) 57, 450 (1965b)
Nagamatsu, A., Hayashida, T.: Hydrolysis of lysine peptides by plasmin. Chem. pharm. Bull. 11, 2680 (1974)
Nagamatsu, A., Okuma, T., Hayashida, T., Yamamura, Y.: Studies on antiplasminic agents. Chem. Pharm. Bull. 16, 211 (1968)
Nagamatsu, A., Okuma, T., Watanabe, M., Yamamura, Y.: The inhibition of plasmin by some amino acid derivatives. J. Biochem. (Tokyo) 54, 491 (1963)
Nagasawa, S., Suzuki, T.: The N-terminal sequence of the light chain derivative of bovine plasmin. Biochem. biophys. Res. Commun. 41, 562 (1970)
Nanninga, L. B.: Rapid determination of Profibrinolysin (plasminogen) in plasma. Thrombos. Diathes. haemorrh. (Stuttg.) 17, 8 (1967)
Nanninga, L. B.: Molar concentrations of fibrinolytic components, especially free fibrinolysin, in vivo. Thrombos. Diathes. haemorrh. (Stuttg.) 33, 244 (1975)
Nanninga, L. B., Guest, M. M.: Activity-pH relationship and Michaelis constants during activation of Profibrinolysin and during fibrinogenolysis. Thrombos. Diathes. haemorrh. (Stuttg.) 19, 492 (1968)
Nolf, P.: Contribution à l’étude de la coagulation du sang. (5e memoire) La fibrinolyse. Arch. int. Physiol. 6, 306 (1908)
Ogston, D., Ogston, C. M., Ratnoff, O. D., Forbes, C. D.: Studies on a complex mechanism for the activation of plasminogen by kaolin and by chloroform. The participation of Hageman factor and additional cofactors. J. clin. Invest. 48, 1786 (1969)
Okamoto, S., Hijikata, A., Kinjo, K., Kikumoto, R., Ohkubo, K., Tonomura, S., Tamao, Y.: A novel series of synthetic thrombin inhibitors having extremely potent and highly selective action. Kobe J. med. Sci. 21, 43 (1975)
Okamoto, U., Yamamoto, J.: A smaller molecule Sk-reactive protein (plasminogen-proactivator) derived from the macromolecule of human plasma fraction I. 5th Congr. Int. Soc. Thromb. Haemostatis, Abstr. 11, Paris 1975
Okano, A., Inaoka, M., Funabashi, S., Iwamoto, M., Isoda, S., Moroi, R., Abiko, Y., Hirata, M.: Medicinal chemical studies on antiplasmin drugs. 4. Chemical modification of trans-4-aminomethylcyclohexanecarboxylic acid and its effect on antiplasmin activity. J. med. Chem. 15, 247(1972)
Oshiba, S., Ariga, T.: Purification and characterization of bilokinase, a biliary plasminogen activator. 5th Congr. Int. Soc. Thromb. Haemostasis, Abstr. 13, Paris 1975
Oshiba, S., Hata, S., Okamoto, S.: Plasminogen activator in mammalian bile. Jap. J. Physiol. 19, 212(1968)
Painter, R. H., Charles, A. F.: Characterization of a soluble plasminogen activator from kidney cell cultures. Amer. J. Physiol. 202, 1125 (1962)
Paoni, N. F., Castellino, F. J.: Isolation of a low molecular weight form of plasminogen. Biochem. biophys. Res. Commun. 65, 757 (1975)
Perlewitz, J., Markwardt, F.: Über die fibrinolytische Aktivität menschlicher Gewebe. Folia haemat. (Lpz.) 92, 46 (1969)
Permin, P. M.: Properties of the fibrinokinase-fibrinolysin system. Nature (Lond.) 160, 571 (1947)
Permin, P. M.: The fibrinolytic activator in animal tissue. Acta physiol. scand. 21, 1959 (1950)
Petkov, D., Christova, E., Pojarlieff, I., Stambolieva, N.: Structure-activity relationship in the urokinase hydrolysis of α-N-acetyl-l-lysine anilides. Europ. J. Biochem. 51, 25 (1975)
Pizza, S. V., Schwartz, M. L., Hill, R. L., McKee, P. A.: The effect of plasmin on the subunit structure of human fibrin. J. biol. Chem. 248, 4574 (1973)
Ploug, J., Kjeldgaard, N. O.: Isolation of plasminogen activator (urokinase) from urine. Arch. Biochem. 62, 500 (1956)
Ploug, J., Kjeldgaard, N. O.: Urokinase, an activator of plasminogen from human urine. I. Isolation and properties. Biochim. biophys. Acta (Amst.) 24, 278 (1957)
Prokopowicz, J.: Purification of plasminogen from human granulocytes using DEAE-Sephadex column chromatography. Biochim. biophys. Acta (Amst.) 154, 91 (1968)
Prokopowicz, J., Rejniak, L., Niewiarowski, S., Worowski, K.: Fibrinolytic activity of tissue sections of dog kidney. Thrombos. Diathes. haemorrh. (Stuttg.) 12, 394 (1964)
Quigley, J. P., Ossowski, L., Reich, E.: Plasminogen, the serum proenzyme activated by factors from cells transformed by oncogenic viruses. J. biol. Chem. 249, 4306 (1974)
Rabiner, S. F., Goldfine, I. C., Hart, A., Summaria, L., Robbins, K. C.: Radioimmunoassay of human plasminogen and plasmin. J. Lab. clin. Med. 74, 265 (1969)
Reddy, K. N. N., Kline, D. L.: Requirement of human plasmin for streptokinase activation of bovine plasminogen. Thrombos. Res. 6, 481 (1975)
Reddy, K. N. N., Markus, G.: Mechanism of activation of human plasminogen by streptokinase. Presence of active center in streptokinase-plasminogen complex. J. biol. Chem. 247, 1683 (1972)
Reddy, K. N. N., Markus, G.: Further evidence for an active center in streptokinase-plasminogen complex; interaction with pancreatic trypsin inhibitor. Biochem. biophys. Res. Commun. 51, 672 (1973)
Reddy, K. N. N., Markus, G.: Esterase activities in the zymogen moiety of the streptokinase-plasminogen complex. J. biol. Chem. 249, 4851 (1974)
Remmert, L. F., Cohen, P.: Partial purification and properties of a proteolytic enzyme of human serum. J. biol. Chem. 181, 431 (1949)
Renzo, E. C. de, Boggiano, E., Barg, W. F., Buck, F. F.: Interaction of streptokinase and human plasminogen. IV. Further gel electrophoretic studies on the combination of streptokinase with human plasminogen or human plasmin. J. biol. Chem. 242, 2428 (1967a)
Renzo, E. C. de, Siiteri, P. K., Hutchings, B. L., Bell, P. H.: Preparation and certain properties of highly purified streptokinase. J. biol. Chem. 242, 533 (1967b)
Rickli, E. E.: The activation mechanism of human plasminogen. Thrombos. Diathes. haemorrh. (Stuttg.) 34, 386 (1975)
Rickli, E. E., Cuendet, P. A.: Isolation of plasmin-free human plasminogen with N-terminal glutamic acid. Biochim. biophys. Acta (Amst.) 250, 447 (1971)
Rickli, E. E., Otavski, W. J.: Release of an N-terminal peptide from human plasminogen during activation with urokinase. Biochim. biophys. Acta (Amst.) 295, 381 (1973)
Rickli, E. E., Zaugg, H.: Isolation and purification of highly enriched tissue plasminogen activator from pig heart. Thrombos. Diathes. haemorrh. (Stuttg.) 23, 64 (1970)
Rifé, U., Shulman, S.: The streptokinase activation of human plasminogen. Direct analysis of the activation mixture. Thrombos. Diathes. haemorrh. (Stuttg.) 10, 133 (1963)
Rifé, U., Shulman, S.: Molecular changes in activation of plasminogen. I. Release of peptide fragments. Biochim. biophys. Acta (Amst.) 86, 317 (1964)
Rifé, U., Shulman, S.: Molecular changes in activation of plasminogen. II. Comparison of peptide liberations during incubation with and without streptokinase. Biochim. biophys. Acta (Amst.) 86, 328 (1964)
Rimon, A., Shamash, J., Shapiro, B.: The plasmin inhibitor of human plasma. IV. Its action on plasmin, trypsin, chymotrypsin and thrombin. J. biol. Chem. 241, 5102 (1966)
Robbins, K. C., Bernabe, P., Arzadon, L., Summaria, L.: The primary structure of human plasminogen. I. The NH2-terminal sequences of human plasminogen and the S-carboxymethyl heavy (A) and light (B) chain derivatives of plasmin. J. biol. Chem. 247, 6757 (1972)
Robbins, K. C., Bernabe, P., Arzadon, L., Summaria, L.: The primary structure of human plasminogen. II. The histidine loop of human plasmin. Light (B) chain active center histidine sequence. J. biol. Chem. 248, 1631 (1973a)
Robbins, K. C., Bernabe, P., Arzadon, L., Summaria, L.: NH2-terminal sequences of mammalian plasminogens and plasmin S-carboxymethyl heavy (A) and light (B) chain derivatives. A reevaluation of the mechanism of activation of plasminogen. J. biol. Chem. 248, 7242 (1973b)
Robbins, K. C., Ling, C. M., Elwyn, D., Barlow, G. H.: Further studies on the purification and characterization of human plasminogen and plasmin. J. Biol. Chem. 240, 541 (1965)
Robbins, K. C., Summaria, L.: Purification of human plasminogen and plasmin by gel filtration and chromatography on diethylaminoethyl-Sephadex. J. biol. Chem. 238, 952 (1963)
Robbins, K. C., Summaria, L.: Human plasminogen and plasmin. In: Methods in enzymology. Vol. XIX : Proteolytic enzymes. New York-London : Academic Press 1970
Robbins, K. C., Summaria, L.: Biochemistry of fibrinolysis. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 47, 9 (1971)
Robbins, K. C., Summaria, L., Hsieh, B., Shah, R. J.: The peptide chains of human plasmin. Mechanism of activation of human plasminogen to plasmin. J. biol. Chem. 242, 2333 (1967)
Roberts, P. S.: Measurement of the rate of plasmin action on synthetic substrates. J. biol. Chem. 232, 285 (1958)
Roberts, P. S.: The esterase activities of human plasmin during purification and subsequent activation by streptokinase or glycerol. J. biol. Chem. 235, 2262 (1960)
Roberts, P. S.: The postulated acetyl esterase activity of streptokinase. Biochim. biophys. Acta (Amst.) 77, 145 (1963)
Roberts, P. S., Burkat, R. K.: The stabilizing effect of neutral salts on plasmin. Biochim. biophys. Acta (Amst.) 113, 193 (1966)
Ronwin, E.: Enzymatic properties of bovine plasmin preparations; evidence for similarity to but non-identity with trypsin. Canad. J. Biochem. 34, 1169 (1956)
Rybak, M., Petakova, M.: Investigations of plasminogen and plasmin by immunoelectrophoresis on fibrin-agar plates. Detection of two plasminogens in human serum. Clin. chim. Acta 8, 133 (1963)
Sahli, W.: Über das Vorkommen von Pepsin und Trypsin im normalen menschlichen Urin. Pflügers Arch. ges. Physiol. 36, 209 (1885)
Sandberg, H., Rezai, M., Bangayan, T. T., Bellet, S., Feinberg, L. J., Hunter, S.: Organ distribution of fibrinolytic activity in man. J. Lab. clin. Med. 61, 592 (1963)
Scheraga, H. A., Ehrenpreis, S., Sullivan, E.: Comparative kinetic behaviour of thrombin, plasmin, and trypsin toward synthetic substrates. Nature (Lond.) 182, 461 (1958)
Schick, L. A., Castellino, F. J.: Interaction of streptokinase and rabbit plasminogen. Biochemistry 12, 4315 (1973)
Schick, L. A., Castellino, F. J.: Direct evidence for the generation of an active site in the plasminogen moiety of the streptokinase-human plasminogen activator complex. Biochem. biophys. Res. Commun. 57, 47 (1974)
Schmitz, A.: Über die Freilegung von aktivem Trypsin aus Blutplasma. Zweite Mitteilung. Zur Kenntnis des Plasma-Trypsin-Systems. Hoppe-Seylers Z. physiol. Chem. 250, 37 (1937)
Schulte, W., Vorbauer, J.: Fibrinolytische Effekte beim Kontakt von Speichel und Blut. Dtsch. Zahn-, Mund- u. Kieferheilkd. 44, 23 (1965)
Schwick, H. G.: Biochemie der Fibrinolyse. Behringwerk-Mitt. Heft 44, 103 (1964)
Schwick, H. G.: Biochemie der Fibrinolyse. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 22, 27 (1967)
Schwick, H. G.: Entwicklungstendenzen immunologischer Methoden in der Klinik. Fresenius Z. analyt. Chem. 243, 424 (1968)
Semar, M., Skoza, L., Johnson, A. J.: Partial purification and properties of a plasminogen activator from human erythrocytes. J. clin. Invest. 48, 1777 (1969)
Sgouris, J. T., Inman, J. K., McCall, K. B.: The preparation of human urokinase. Amer. J. Cardiol. 6,406(1960)
Sgouris, J. T., Storey, R. W., McCall, K. B., Anderson, H. D.: The purification, assay, sterilization, and removal of pyrogenicity of human urokinase. Vox Sang. (Basel) 7, 739 (1962)
Sherry, S.: The fibrinolytic activity of streptokinase activated human plasmin. J. clin. Invest. 33, 1054 (1954)
Sherry, S.: Present concept of the fibrinolytic mechanism. Scand. J. haemat. 7, 70 (1965)
Sherry, S.: Fibrinolysis. Ann. Rev. Med. 19, 247 (1968)
Sherry, S., Alkjaersig, N.: Studies on the activation of human plasminogen. J. clin. Invest. 35, 735 (1956)
Sherry, S., Alkjaersig, N., Fletcher, A. P.: Assay of urokinase preparations with the synthetic substrate acetyl-l-lysine methyl ester. J. Lab. clin. Med. 64, 145 (1964)
Sherry, S., Alkjaersig, N., Fletcher, A. P.: Comparative study of thrombin on substituted arginine and lysine esters. Amer. J. Physiol. 209, 577 (1965)
Sherry, S., Alkjaersig, N., Fletcher, A. P.: Activity of plasmin and streptokinase activator on substituted arginine and lysine esters. Thrombos. Diathes. haemorrh. (Stuttg.) 18, 18 (1966)
Sherry, S., Fletcher, A. P., Alkjaersig, N.: Fibrinolysis and fibrinolytic activity in man. Physiol. Rev. 39, 343 (1959)
Siefring, G. E., Castellino, F. J.: The role of sialic acid in the determination of distinct properties of the isozymes of rabbit plasminogen. J. biol. Chem. 249, 7742 (1974)
Silverstein, R. M.: The plasmin-catalyzed hydrolysis of Nα-cbz-l-lysine p-nitrophenyl ester. Thrombos. Res. 3, 729 (1973)
Silverstein, R. M.: Determination of human plasminogen using Nα-CBZ[carbobenzyloxy]-l-lysine p-nitrophenyl ester as substrate. Analyt. Biochem. 65, 500 (1975)
Sjöholm, I., Wiman, B., Wallén, P.: Studies on the conformational changes of plasminogen induced during activation to plasmin and by 6-aminohexanoic acid. Europ. J. Biochem. 39, 471 (1973)
Slotta, K. H., Gonzales, J. D.: Native plasminogen. Biochemistry 3, 285 (1964)
Slotta, K. H., Michel, H., Santos, B. G.: Comparative studies on native and acid treated plasminogens. Biochim. biophys. Acta (Amst.) 58, 459 (1962)
Smillie, L. B., Furka, A., Nagabushan, N., Stevenson, K. J., Parkes, C. O.: Structure of chymotrypsinogen B compared with chymotrypsinogen A and trypsinogen. Nature (Lond.) 218, 343 (1968)
Smyrniotis, F. E., Fletcher, A. P., Alkjaersig, N., Sherry, S.: Urokinase excretion in health and its alteration in certain disease states. Thrombos. Diathes. haemorrh. (Stuttg.) 3, 257 (1959)
Sobel, G. W., Mohler, S. R., Jones, N. W., Dowdy, A. B. C., Guest, M. M.: Urokinase: an activator of plasma Profibrinolysin extracted from urine. Amer. J. Physiol. 171, 768 (1952)
Sodetz, J. M., Brockway, W. J., Castellino, F. J.: Multiplicity of rabbit plasminogen. Physical characterization. Biochemistry 11, 4451 (1972)
Sodetz, J. M., Brockway, W. J., Mann, K. G., Castellino, F. J.: The mechanism of activation of rabbit plasminogen by urokinase. Lack of a preactivation peptide. Biochem. biophys. Res. Commun. 60, 729 (1974)
Sodetz, J. M., Castellino, F. J.: A comparison of steady and presteady state kinetics of bovine and human plasmin. Biochemistry 11, 3167 (1972)
Sodetz, J. M., Castellino, F. J.: The mechanism of activation of rabbit plasminogen by urokinase. J. biol. Chem. 250, 3041 (1975)
Sottrup-Jensen, L., Zajdel, M., Claeys, H., Petersen, T. E., Magnusson, S.: Amino acid sequence of activation cleavage site in plasminogen : Homology with “pro” part of prothrombin. Proc. nat. Acad. Sci. (Wash.) 72, 2577 (1975)
Soru, E.: Thin layer chromatography of staphylokinase activated human plasmin. Purification of human plasmin by serial molecular sieve chromatography on Polyacrylamide. Rev. Roum. Biochimie 5, 17(1968)
Spritz, N., Cameron, D. J.: Streptokinase induced lysine-methyl-esterase activity of human euglobulin. Proc. Soc. exp. Biol. (N.Y.) 109, 848 (1962)
Storm, O.: Fibrinolytic activity in human tears. Scand. J. clin. Lab. Invest. 7, 55 (1955)
Stroud, R. M., Kay, L. M., Dickerson, R. E.: The structure of bovine trypsin: Electron density maps of the inhibited enzyme at 5 Å and at 2.7 Å resolution. J. molec. Biol. 83, 185 (1974)
Stürzebecher, J., Markwardt, F., Richter, P., Wagner, G., Walsmann, P., Landmann, H.: Synthetische Inhibitoren von Serinproteinasen. 3. Mitteilung: Über die Hemm Wirkung basisch substituierter Phenylcarbonsäureester gegenüber Trypsin, Plasmin und Thrombin. Pharmazie 29, 337 (1974)
Summaria, L., Arzadon, L., Bernabe, P., Robbins, K. C.: Studies on the isolation of the multiple molecular forms of human plasminogen and plasmin by isoelectric focusing methods. J. biol. Chem. 247, 4691 (1972)
Summaria, L., Arzadon, L., Bernabe, P., Robbins, K. C.: Isolation, characterization, and comparison of the S-carboxy methyl heavy (A) and light (B) chain derivatives of cat, dog, rabbit, and bovine plasmins. J. biol. Chem. 248, 6522 (1973)
Summaria, L., Arzadon, L., Bernabe, P., Robbins, K. C.: The interaction of streptokinase with human, cat, dog, and rabbit plasminogen. The fragmentation of streptokinase in the equimolar plasminogen-streptokinase complexes. J. biol. Chem. 249, 4760 (1974)
Summaria, L., Arzadon, L., Bernabe, P., Robbins, K. C.: The activation of plasminogen to plasmin in the presence of the plasmin inhibitor Trasylol. The preparation of plasmin with the same NH2-terminal heavy (A) chain sequence as the parent zymogen. J. biol. Chem. 250, 3988 (1975)
Summaria, L., Hsieh, B., Groskopf, W. R., Robbins, K. C.: Direct activation of human plasminogen by streptokinase. Proc. Soc. exp. Biol. (N.Y.) 130, 737 (1969)
Summaria, L., Hsieh, B., Groskopf, W. R., Robbins, K. C., Barlow, G. H.: The isolation of the S-carboxymethyl β-(light)-chain derivative of human plasmin. The localization of the active site on the light chain. J. biol. Chem. 242, 5046 (1967b)
Summaria, L., Hsieh, B., Robbins, K. C.: The specific mechanism of activation of human plasminogen to plasmin. J. biol. Chem. 242, 4279 (1967a)
Summaria, L., Ling, C.-M., Groskopf, W. R., Robbins, K. C.: The active site of bovine plasminogen activator. Interaction of streptokinase with human plasminogen and plasmin. J. biol. Chem. 243, 144(1968)
Summaria, L., Robbins, K. C., Barlow, G. H.: Dissociation of the equimolar human plasmin-streptokinase complex. Partial characterization of the isolated plasmin and streptokinase moieties. J. biol. Chem. 246, 2136 (1971a)
Summaria, L., Robbins, K. C., Barlow, G. H.: Isolation and characterization of the S-carboxymethyl heavy chain derivative of human plasmin. J. biol. Chem. 246, 2143 (1971b)
Sweet, B., McNicol, G. P., Douglas, A. S.: In vitro studies of staphylokinase. Clin. Sci. 29, 375 (1965)
Szczeklik, E., Orlowski, M., Szczeklik, A., Narczewska, B.: The activity of plasma, serum, thrombin, and plasmin toward synthetic trypsin substrates. Thrombos. Diathes. haemorrh. (Stuttg.) 19, 99 (1968)
Takada, A., Takada, Y., Ambrus, J. L.: Streptokinase-activatable proactivator of human and bovine plasminogen. J. biol. Chem. 245, 6389 (1970)
Takada, A., Takada, Y., Ambrus, J. L.: Proactivators in the fibrinolysin system. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 47, 37 (1971)
Takada, A., Takada, Y., Ambrus, J. L.: Further studies of plasminogen proactivator. Biochim. biophys. Acta (Amst.) 263, 610 (1972)
Tangen, O., Wik, K. O., Almqvist, I. A. M., Arfors, K. E., Hint, H. C.: Effects of dextran on the structure and plasmin-induced lysis of human fibrin. Thrombos. Res. 1, 487 (1972)
Taylor, F. B., Beisswenger, J. G.: Identification of modified streptokinase as the activator of bovine and human plasminogen. J. biol. Chem. 248, 1127 (1973)
Taylor, F. B., Botts, J.: Purification and characterization of streptokinase with studies of streptokinase activation of plasminogen. Biochemistry 7, 232 (1968)
Taylor, F. B., Tomar, R. H.: Streptokinase. In: Methods in enzymology. Vol. XIX: Proteolytic enzymes. New York-London : Academic Press 1970
Thorsen, S., Müllertz, S.: Rate of activation and electrophoretic mobility of unmodified and partially degraded plasminogen. Effects of 6-aminohexanoic acid and related compounds. Scand. J. clin. Lab. Invest. 34, 167 (1974)
Tillett, W. S., Garner, R. L.: The fibrinolytic activity of hemolytic streptococci. J. exp. Med. 58, 485 (1933)
Todd, A. S.: The histological localization of fibrinolytic activator. J. Path. Bact. 78, 281 (1959)
Todd, A. S.: Localization of fibrinolytic activity in tissues. Brit. med. Bull. 20, 210 (1964)
Tomar, R. H.: Streptokinase: preparation, comparison with streptococcal proteinase, and behavior as a trypsin substrate. Proc. Soc. exp. Biol. (N.Y.) 127, 239 (1968)
Tomar, R. H., Taylor, F. B.: The streptokinase-human plasminogen activator complex. Composition and identity of a subcomponent with activator activity. Biochem. J. 125, 793 (1971)
Troll, W., Sherry, S.: The activation of human plasminogen by streptokinase. J. biol. Chem. 213, 881 (1955)
Troll, W., Sherry, S., Wachmann, J.: The action of plasmin on synthetic substrates. J. biol. Chem. 208, 85 (1954)
Ts’ao, C. H., Kline, D. L.: Plasminogen activator by reaction of streptokinase with human plasminogen. J. appl. Physiol. 26, 634 (1969)
Tyler, H. M.: Fibrin crosslinking demonstrated by thrombelastography. Thrombos. Diathes. haemorrh. (Stuttg.) 22, 398 (1969)
Tympanidis, K., Astrup, T.: Fibrinolytic activity of epithelium of bladder of rat and man. J. Urol. (Baltimore) 105, 214 (1971)
Umezawa, H.: Enzyme inhibitors of microbial origin. Baltimore: Univ. Press 1972
Unkeless, J., Danø, K., Kellerman, G. M., Reich, E.: Fibrinolysis associated with oncogenic transformation. Partial purification and characterization of the cell factor, a plasminogen activator. J. biol. Chem. 249, 4295 (1974)
Vaux Saint-Cyr, C. de: Mise en évidence de constituants possédant une activité estérasique dans les préparations de streptokinase. C.R. Soc. Biol. (Paris) 254, 3749 (1962)
Vesterberg, K., Vesterberg, O.: Staphylokinase. J. med. Microbiol. 5, 441 (1972)
Vigorito, T. F., Celander, E., Celander, D. R.: The origin of urokinase. Fed. Proc. 24, 512 (1965)
Vogel, R., Trautschold, L, Werle, E.: Natürliche Proteinasen-Inhibitoren. In: Biochemie und Klinik. Stuttgart: Thieme 1966
Wallén, P.: Studies on the purification of human plasminogen. I. The preparation of a partially purified human plasminogen with a low spontaneous proteolytic activity. Ark. Kemi 19, 451 (1962a)
Wallén, P.: Studies on the purification of human plasminogen. II. Further purification of human plasminogen on cellulose ion exchangers and by means of gel filtration on Sephadex. Ark. Kemi 19, 469 (1962b)
Wallén, P., Bergström, K.: Action of thrombin on plasmin digested fibrinogen. Acta chem. scand. 12, 574(1958)
Wallén, P., Bergström, K.: Effect of lysine on the purification of human plasminogen on cellulose ion exchangers. Acta chem. scand. 13, 1464 (1959)
Wallén, P., Bergström, K.: Purification of human plasminogen on DEAE-cellulose. Acta chem. scand. 14, 217 (1960)
Wallén, P., Iwanaga, S.: Differences between plasmic and tryptic digests of human S-sulfo fibrinogen. Biochim. biophys. Acta (Amst.) 221, 20 (1968)
Wallén, P., Wiman, B.: Characterization of human plasminogen. I. On the relationship between different molecular forms of plasminogen demonstrated in plasma and found in purified preparations. Biochim. biophys. Acta (Amst.) 221, 20 (1970)
Wallén, P., Wiman, B.: Characterization of human plasminogen. II. Separation and partial characterization of different molecular forms of human plasminogen. Biochim. biophys. Acta (Amst.) 257, 122(1972)
Wallenbeck, I. A. M., Tangen, O.: Lysis of fibrin formed in the presence of dextran and other macromolecules. Thrombos. Res. 6, 75 (1975)
Walsmann, P., Horn, H., Landmann, H., Markwardt, F., Stürzebecher, J., Wagner, G.: Synthetische Inhibitoren der Serinproteinasen. 5. Mitteilung: Über die Hemmung von Trypsin, Plasmin und Thrombin durch araliphatische Amidinoverbindungen mit Ätherstruktur sowie Ester der 3- und 4-Amidinophenoxyessigsäure. Pharmazie 30, 386 (1975)
Walsmann, P., Landmann, H., Markwardt, F., Stürzebecher, J., Vieweg, H., Wagner, G.: Synthetische Inhibitoren der Serinproteinasen. 3. Mitteilung : Über die Hemmwirkung substituierter Anilide der 3- und 4-Amidinobenzoesäuren und Amidinoanilide verschiedener Benzoe- und Benzolsulfonsäuren. Pharmazie 29, 405 (1974b)
Walsmann, P., Markwardt, F., Richter, P., Stürzebecher, J., Wagner, G., Landmann, H.: Synthetische Inhibitoren von Serinproteinasen. 2. Mitteilung: Über die Hemmung von Homologen der Amidinobenzoesäuren und ihrer Ester gegenüber Trypsin, Plasmin und Thrombin. Pharmazie 29, 333 (1974a)
Walther, P. J., Steinman, H. M., Hill, R. L., McKee, P. A.: Activation of human plasminogen by urokinase. J. biol. Chem. 249, 1173 (1974)
Walton, P. L.: The hydrolysis of α-N-acetylglycyl-l-lysine methyl ester by urokinase. Biochim. biophys. Acta (Amst.) 132, 104 (1967)
Warren, B. A.: Fibrinolytic activity of vascular endothelium. Brit. med. Bull. 20, 213 (1964)
Weinstein, M. J., Doolittle, R. F.: Differential specificities of thrombin, plasmin, and trypsin with regard to synthetic and natural substrates and inhibitors. Biochim. biophys. Acta (Amst.) 258, 577 (1972)
Werkheiser, W. C., Markus, G.: The interaction of streptokinase with human plasminogen. II. The kinetics of activation. J. biol. Chem. 239, 2644 (1964)
White, W. F., Barlow, G. H.: Urinary plasminogen activator (urokinase). In: Methods in enzymol-ogy, Vol.XIX: Proteolytic enzymes. New York-London: Academic Press 1970
White, W. F., Barlow, G. H., Mozen, M. M.: The isolation and characterization of plasminogen activators (urokinase) from human urine. Biochemistry 5, 2160 (1966)
Williams, J. R. B.: The fibrinolytic activity of urine. Brit. J. exp. Path. 32, 530 (1951)
Wiman, B.: Structure of the N-terminal fragment of human plasminogen obtained after cleavage with cyanogen bromide. Thrombos. Res. 1, 89 (1972)
Wiman, B.: Primary structure of peptides released during activation of human plasminogen by urokinase. Europ. J. Biochem. 39, 1 (1973)
Wiman, B., Wallén, P.: Activation of human plasminogen by an insoluble derivative of urokinase. Structural changes of plasminogen in the course of activation of plasmin and demonstration of a possible intermediate compound. Europ. J. Biochem. 36, 25 (1973)
Wiman, B., Wallén, P.: On the primary structure of human plasminogen and plasmin, cyanogen bromide fragments. 5th Congr. Int. Soc. Thromb. Haemostasis, Abstr. 109, Paris 1975 a
Wiman, B., Wallén, P.: Amino acid sequence around the arginyl-valyl bond in plasminogen which is cleaved during the second step of the activation process. Thrombos. Res. 7, 239 (1975b)
Wiman, B., Wallén, P.: Structural relationship between “glutamic acid” and “lysine” forms of human plasminogen and their interaction with the NH2-terminal activation peptide as studied by affinity chromatography. Europ. J. Biochem. 50, 489 (1975c)
Wiman, B., Wallén, P.: On the primary structure of human plasminogen and plasmin. Purification and characterization of cyanogen-bromide fragments. Europ. J. Biochem. 57, 387 (1975d)
Wiman, B., Wallén, P.: Amino-acid sequence of the cyanogen-bromide fragment from human plasminogen that forms the linkage between the plasmin chains. Europ. J. Biochem. 58, 539 (1975e)
Wulf, R. J., Mertz, E. T.: Plasminogen VIII. Species specificity of streptokinase. Canad. J. Biochem. 47, 927 (1969)
Yamamoto, J., Nagamatsu, Y.: Low molecular weight proactivator of plasminogen derived from the macromolecular one by lysine-Sepharose chromatography. Nippon Seirigaku Zasshi 36, 176 (1974)
Zylber, J., Blatt, W. F., Jensen, H.: Mechanism of bovine plasminogen activation by human plasmin and streptokinase. Proc. Soc. exp. Biol. (N.Y.) 102, 755 (1959)
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1978 Springer-Verlag Berlin · Heidelberg
About this chapter
Cite this chapter
Landmann, H. (1978). Biochemistry of the Factors of the Fibrinolytic System. In: Markwardt, F. (eds) Fibrinolytics and Antifibrinolytics. Handbuch der experimentellen Pharmakologie / Handbook of Experimental Pharmacology, vol 46. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-66863-0_1
Download citation
DOI: https://doi.org/10.1007/978-3-642-66863-0_1
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-66865-4
Online ISBN: 978-3-642-66863-0
eBook Packages: Springer Book Archive