The mechanism of blood coagulation

  • P. A. Owren
  • H. Stormorken
Conference paper
Part of the Ergebnisse der Physiologie, biologischen Chemie und experimentellen Pharmakologie book series (ERGEBPHYSIOL, volume 68)


Factor VIII Factor Versus Hageman Factor Tissue Thromboplastin Intrinsic Clotting System 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Aas, K.: Prokonvertin og konvertin. Undersøkelser over blodets koagulasjon med spesielt henblikk på prokonvertin og konvertin. Thesis. Akad. trykningssental Oslo 1952, p. 351.Google Scholar
  2. Abildgaard, U., Purification of two progressive antithrombins of human plasma. Scand. J. clin. Lab. Invest. 19, 190 (1967).Google Scholar
  3. Abildgaard, U.: Highly purified antithrombin III with heparin cofactor activity prepared by disc electrophoresis. Scand. J. clin. Lab. Invest. 21, 89 (1968).PubMedGoogle Scholar
  4. Abildgaard, U.: Binding of thrombin to antithrombin III. Scand. J. clin. Lab. Invest. 24, 23 (1969).PubMedGoogle Scholar
  5. Addis, T.: The pathogenesis of hereditary haemophilia. J. Path. Bact. 15, 427 (1911).Google Scholar
  6. Aggeler, P. M., White, S. G., Glendening, M. B., Page, E. W., Leake, T. B., Bates, G.: Plasma thromboplastin component (PTC) deficiency: a new disease resembling haemophilia. Proc. Soc. exp. Biol. (N.Y.) 79, 692 (1952).PubMedGoogle Scholar
  7. Alexander, B.: Some biochemical, physicochemical and immunochemical studies of prothrombin and proconvertin (factor VII): their biopathologic significance. In: Blood clotting factors (E. Deutsch, ed.), p. 37. London: Pergamon Press 1958.Google Scholar
  8. Alexander, B., Colman, R.: Evidence for a new serum thromboplastic factor. Thrombos. Diathes. haemorrh. (Stuttg.) 4, (Suppl.), 66 (1959).Google Scholar
  9. Alexander, B., de Vries, A., Goldstein, R., Landwehr, G.: Prothrombin conversion accelerator in serum. Science 109, 544 (1949).Google Scholar
  10. Alexander, B., Goldstein, R., Landwehr, G., Cook, C. D.: Congenital SPCA deficiency: a hitherto unrecognized coagulation defect with hemorrhage rectified by serum and serum fractions. J. clin. Invest. 30, 596 (1951).PubMedGoogle Scholar
  11. Altman, R., Hemker, H. C.: Contact activation in the extrinsic blood clotting system. Thrombos. Diathes. haemorrh. (Stuttg.) 18, 525 (1967).Google Scholar
  12. Aoki, N., Harmison, C. R., Seegers, W. H.: Properties of bovine Ac-globulin concentrates and methods of preparation. Canad. J. Biochem. 41, 2409 (1963).PubMedGoogle Scholar
  13. Arthus, M., Pages, C.: Nouvelle théorie chimique de la coagulation du sang. Arch. Physiol. norm. path. 2, 739 (1890).Google Scholar
  14. Bailey, K., Bettelheim, F. R., Lorand, L., Middlebrook, W. R.: Action of thrombin in the clotting of fibrinogen. Nature (Lond.) 167, 233 (1951).PubMedGoogle Scholar
  15. Bang, N. U.: A molecular structural model of fibrin based on electron microscopy of fibrin polymerization. In: Fibrinogen and fibrin. Turnover of clotting factors. Thrombos. Diathes. haemorrh. (Stuttg.) 13 (Suppl.), 73 (1964).Google Scholar
  16. Bangham, A. D.: A correlation between surface charge and coagulant action of phospholipids. Nature (Lond.) 192, 1197 (1961).PubMedGoogle Scholar
  17. Barnhart, M. J., Cress, D. C., Noonan, S. M., Walsh, R. T.: Influence of fibrinolytic products on hepatic release and synthesis of fibrinogen. Thrombos. Diathes. haemorrh. (Stuttg.) 39 (Suppl.), 143 (1970).Google Scholar
  18. Barrow, E. M., Amos, S., Graham, J. B.: Certain biochemical properties of human AHF (Factor 8) separated from fibrinogen with manganous chloride and thrombin. J. Lab. clin. Med. 68, 803 (1966).PubMedGoogle Scholar
  19. Barrow, E. M., Graham, J. B.: Kidney antihemophilic factor. Partial purification and some properties. Biochemistry 7, 3917 (1968).PubMedGoogle Scholar
  20. Barton, P. G.: Sequence theories of blood coagulation reevaluated with reference to lipid-protein interaction. Nature (Lond.) 215, 1508 (1967).PubMedGoogle Scholar
  21. Barton, P. G., Hanahan, D. J.: The preparation and properties of a stable factor V from bovine plasma. Biochim. biophys. Acta (Amst.) 133, 506 (1967).PubMedGoogle Scholar
  22. Barton, P. G., Jackson, C. M., Hanahan, D. J.: Relation between factor V and activated factor X in the generation of prothrombinase. Nature (Lond.) 214, 923 (1967).PubMedGoogle Scholar
  23. Bergsagel, D. E., Nockolds, E. R.: The activation of proaccelerin. Brit. J. Haemat. 11, 395 (1965).Google Scholar
  24. Bergström, D., Wallén, P.: Removal of contaminating plasminogen from purified bovine fibrinogen. Arkiv Kemi 17, 503 (1961).Google Scholar
  25. Bettelheim, F. R., Bailey, K.: The products of the action of thrombin on fibrinogen. Biochim. biophys. Acta (Amst.) 9, 578 (1952).PubMedGoogle Scholar
  26. Biggs, R.: Report on the standardization of the one-stage prothrombin time for the control of anticoagulant therapy. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 17, 303 (1965).Google Scholar
  27. Biggs, R.: Proposal for the use of a preliminary trial reference preparation of thromboplastin for standardizing the one-stage prothrombin time for the control of anti-coagulant therapy. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 39, 363 (1970).Google Scholar
  28. Biggs, R., Bidwell, E.: An attempt to identify a single phospholipid active in blood coagulation. Brit. J. Haemat. 3, 387 (1957).PubMedGoogle Scholar
  29. Biggs, R., Denson, K. W. E.: Second report on the standardization of the one-stage prothrombin time for the control of anticoagulant therapy. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 20, 345 (1966).Google Scholar
  30. Biggs, R., Denson, K. W. E.: Standardization of the one-stage prothrombin-time of anticoagulant therapy. Brit. med. J. 1967 I, 84.Google Scholar
  31. Biggs, R., Denson, K. W. E., Akman, N., Borrett, R., Hadden, M.: Antithrombin III, antifactor Xa and heparin. Brit. J. Haemat. 19, 283 (1970).PubMedGoogle Scholar
  32. Biggs, R., Douglas, A. S., Macfarlane, R. G.: The formation of thromboplastin in human blood. J. Physiol. (Lond.) 119, 89 (1953a).PubMedGoogle Scholar
  33. Biggs, R., Douglas, A. S., Macfarlane, R. G.: The initial stages of blood coagulation. J. Physiol. (Lond.) 122, 538 (1953b).PubMedGoogle Scholar
  34. Biggs, R., Douglas, A. S., Macfarlane, R. G., Dacie, J. V., Pitney, W. R., Merskey, C., O’Brien, J. R.: Christmas disease: a condition previously mistaken for haemophilia. Brit. med. J. 1952 II, 1378.Google Scholar
  35. Biggs, R., Macfarlane, R. G., eds.: Human blood coagulation and its disorders, p. 474. Oxford: Blackwell 1962.Google Scholar
  36. Biggs, R., Macfarlane, R. G., Denson, K. W. E., Ash, B. J.: The interaction of factors VIII and IX. Brit. J. Haemat. 11, 276 (1965).PubMedGoogle Scholar
  37. Biggs, R., Matthews, J. M.: The treatment of haemorrhage in von Willebrand’s disease and the blood level of factor VIII (AHG). Brit. J. Haemat. 9, 203 (1963).PubMedGoogle Scholar
  38. Biggs, R., Sharp, A. A., Margolis, J., Hardisty, R. M., Stewart, J., Davidson, W. M.: Defects in the early stages of blood coagulation: a report of four cases. Brit. J. Haemat. 4, 177 (1958).PubMedGoogle Scholar
  39. Blainville, de: 1834. Quoted by Nygaard, K. K.: Hemorrhagic diseases. St. Louis 1941.Google Scholar
  40. Blombäck, B.: Fibrinogen to fibrin transformation. In: Blood clotting enzymology, ed. W. H. Seegers, p. 143. New York: Acad. Press Inc. 1967.Google Scholar
  41. Blombäck, B., Birger, M., Hessel, B., Iwanaga, S., Reuterby, J., Blombäck, M.: Primary structure of human fibrinogen and fibrin. I. Cleavage of fibrinogen with cyanogen bromide. Isolation and characterization of NH2-terminal fragments of the α (“A”) chain. J. biol. Chem. 247, 1496 (1972).PubMedGoogle Scholar
  42. Blombäck, B., Blombäck, M.: Purification of human and bovine fibrinogen. Arkiv Kemi 10, 415 (1956).Google Scholar
  43. Blombäck, B., Blombäck, M.: A method for the assay of factor V. Scand. J. clin. Lab. Med. 15, 639 (1963).Google Scholar
  44. Blombäck, B., Blombäck, M.: The formation of the fibrin clot from fibrinogen. In: Human blood clotting, ed. Hemker et al., p. 7. Leiden: University Press 1969.Google Scholar
  45. Blombäck, B., Blombäck, M., Deman, P. et al.: Human fibrinopeptides. Isolation, characterization and structure. Biochim. biophys. Acta (Amst.) 115, 371 (1966).PubMedGoogle Scholar
  46. Blombäck, B., Blombäck, M., Henschen, A., Hessel, B., Iwanaga, S., Woods, R.: N-terminal disulphide knot of human fibrinogen. Nature (Lond.) 218, 130 (1968).PubMedGoogle Scholar
  47. Blombäck, B., Blombäck, M., Mammen, E. F., Prasad, A. S.: Fibrinogen Detroit—a molecular defect in the N-terminal disulphide knot of human fibrinogen? Nature (Lond.) 218, 134 (1968).PubMedGoogle Scholar
  48. Blombäck, B., Blombäck, M., Nilsson, I. M.: Note on the purification of human antihemophilic globulin. Acta chem. scand. 12, 1878 (1958).Google Scholar
  49. Blombäck, B., Yamashina, J.: On the N-terminal amino acids in fibrinogen and fibrin. Arkiv Kemi 12, 299 (1958).Google Scholar
  50. Blombäck, M.: Purification of antihaemophilic globulin. Arkiv Kemi 12, 387 (1958).Google Scholar
  51. Blombäck, M., Blombäck, B.: Hemophilia and other haemorrhagic states, p. 242. Chapel Hill Univ. N. Carolina Press 1970.Google Scholar
  52. Borchgrevink, C. F., Owren, P. A.: The hemostatic effect of normal platelets in hemophilia and factor V deficiency. Acta med. scand. 170, 375 (1961).PubMedGoogle Scholar
  53. Bordet, J., Delange, L.: Sur la nature du cytozyme. Recherches sur la coagulation du sang. Ann. Inst. Pasteur 27, 341 (1913).Google Scholar
  54. Bordet, J., Delange, L.: Analyse et synthese du processus de la coagulation. Ann. Soc. roy. Sci. méd. nat. Brux. 72, 87 (1914).Google Scholar
  55. Bordet, J., Gengou, O.: Recherches sur la coagulation du sang: contribution de l’étude du plasma fluore. Ann. Inst. Pasteur 17, 822 (1903).Google Scholar
  56. Bordet, J., Gengou, O.: Recherches sur la coagulation du sang et les serum anticoagulants. Ann. Inst. Pasteur 18, 98 (1904).Google Scholar
  57. Botti, R. E., Ratnoff, O. D.: Studies on the pathogenesis of thrombosis: An experimental “hypercoagulable” state induced by the intravenous injection of ellagic acid. J. Lab. clin. Med. 64, 385 (1964).PubMedGoogle Scholar
  58. Bouma, B. N., Wiegerinck, Y., Sixma, J. J., Mourik, J. A., van, Mochtar, I. A.: Immunological characterization of purified antihaemophilic factor A (factor VIII) which corrects abnormal platelet retention in von Willebrand’s disease. Nature (Lond.) New Biol. 236, 104 (1972).Google Scholar
  59. Breckenridge, R. T., Hoyer, L. W.: The hererogeneity of hemophilia. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 43, 5 (1971).Google Scholar
  60. Breckenridge, R. T., Ratnoff, O. D.: Studies on the site of action of circulating anticoagulant in disseminated lupus erythematosus. Evidence that this anticoagulant inhibits the reaction between activated Stuart factor (factor X) and proaccelerin (factor V). Amer. J. Med. 35, 813 (1963).PubMedGoogle Scholar
  61. Breckenridge, R. T., Ratnoff, O. D.: Studies on the anticoagulant action of soybean trypsin inhibitor. Clin. Res. 12, 221 (1964).Google Scholar
  62. Breckenridge, R. T., Ratnoff, O. D.: The activation of human proaccelerin (Factor V). Thrombos. Diathes. haemorrh. (Stuttg.) 17, 217 (1965).Google Scholar
  63. Brinkhous, K. M.: A study of the clotting time in hemophilia: the delayed formation of thrombin. Amer. J. med. Sci. 198, 509 (1939).Google Scholar
  64. Brinkhous, K. M., Shanbrom, E., Roberts, H. R., Webster, W. P., Fekete, L., Wagner, R. H.: A new high potency glycine precipitated antihemophilic factor (AHF) concentrate. Treatment of classical hemophilia and hemophilia with inhibitors. J. Amer. med. Ass. 205, 613 (1968).Google Scholar
  65. Brinkhous, K. M., Smith, H. P., Warner, E. D., Seegers, W. H.: The inhibition of blood clotting: an unidentified substance which acts in conjunction with heparin to prevent the conversion of prothrombin into thrombin. Amer. J. Physiol. 125, 683 (1939).Google Scholar
  66. Brown, M., Rothstein, F.: Fibrinogen from human plasma: Preparation by precipitation with heavy-metal coordination complex. Science 155, 1017 (1967).PubMedGoogle Scholar
  67. Buchanan, A.: On the coagulation of the blood and other fibrinoferous liquids. J. Physiol. (Lond.) 2, 158 (1879). (Reprinted from London Med. Gazette, 1845, 1, 617.)Google Scholar
  68. Bulloch, W., Fildes, P.: Treasury of human inheritance. Parts V and VI. Section XIVa. Haemophilia. London: Kulau and Co., Limited, 1911.Google Scholar
  69. Buluk, K., Januszko, T., Olbromski, J.: Conversion of fibrin to desmofibrin. Nature (Lond.) 191, 1093 (1961).Google Scholar
  70. Buluk, K., Olbromski, J., Januszko, T., Zuch, A.: Desmofibrin formation and the activity of the fibrin stabilizing factor (FSF) during the cleavage of its SH groups by thrombin. Thrombos. Diathes. haemorrh. (Stuttg.) 16, 51 (1966).Google Scholar
  71. Burstein, M.: Sur l’activation de la thrombin par le plasma héparine. Arch. int. Pharmacodyn. 101, 285 (1955).PubMedGoogle Scholar
  72. Caldwell, M. J., Kaulla, K. N., von, Seegers, W. H.: Procoagulant material from human urine in prothrombin activation. Thrombos. Diathes. haemorrh. (Stuttg.) 9, 53 (1963).Google Scholar
  73. Capet-Antonini, F., Guinand, S.: Effet de la température sur la structure du fibrinogene. C. R. Acad. Sci. (Paris) 265, 2093 (1967).Google Scholar
  74. Caspary, E. A., Kekwick, R. A.: Some physicochemical properties of human fibrinogen. Biochem. J. 67, 41 (1957).PubMedGoogle Scholar
  75. Chargaff, E.: The coagulation of blood. Advanc. Enzymol. 5, 31 (1945).Google Scholar
  76. Chargaff, E., Bendich, A., Cohen, S. S.: The thromboplastic protein: structure, properties, disintegration. J. biol. Chem. 156, 161 (1944).Google Scholar
  77. Clegg, J. B., Bailey, K.: The separation and isolation of the peptide chains of fibrin. Biochim. biophys. Acta (Amst.) 63, 525 (1962).PubMedGoogle Scholar
  78. Cohen, C., Slayter, H., Goldstein, L., Kucera, J., Hall, C.: Polymorphism in fibrinogen aggregates. J. molec. Biol. 22, 385 (1966).PubMedGoogle Scholar
  79. Cohn, E. J., Strong, L. E., Hughes, W. L., Jr., Mulford, D. J., Ashworth, J. N., Melin, M., Taylor, H. L.: Preparation and properties of serum and plasma proteins. IV. A system for the separation into fractions of the protein and lipoprotein components of biological tissues and fluids. J. Amer. chem. Soc. 68, 459 (1946).Google Scholar
  80. Connor, W. E., Warner, E. D., Carter, J. R.: A labile serum factor clotting defect: its demonstration by the thromboplastin generation test and its clinical significance. J. clin. Invest. 40, 13 (1961).PubMedGoogle Scholar
  81. Cox, F. M., Lanchantin, G. F., Ware, A. G.: Chromatographic purification of human serum accelerator globulin. J. clin. Invest. 35, 106 (1956).PubMedGoogle Scholar
  82. Davie, E. W., Hougie, C., Lundblad, R. L.: The mechanism of blood coagulation. In: Recent advances in blood coagulation, ed. Poller, J. V. A., p. 13. London: Churchill 1969.Google Scholar
  83. Denis, P. S.: Memoire sur le sang. Paris 1859.Google Scholar
  84. Denson, K. W. E.: Structurally defective forms of factor VIII, factor IX and factor X. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 43, 19 (1971).Google Scholar
  85. Denson, K. W. E., Biggs, R., Haddon, M. E., Borret, E., Cobb, K.: Two types of haemophilia (A+ and A-). A study of 48 cases. Brit. J. Haemat. 17, 163 (1969).PubMedGoogle Scholar
  86. Denson, K. W. E., Biggs, R., Mannucci, P. M.: An investigation of three patients with Christmas disease due to an abnormal type of factor IX. J. clin. Path. 21, 160 (1968).PubMedGoogle Scholar
  87. Denson, K. W. E., Lurie, E. A., De Cataldo, F. D. E., Mannucci, P. M.: Factor X defect. Recognition of abnormal forms of factor X. Brit. J. Haemat. 18, 317 (1970).PubMedGoogle Scholar
  88. Desai, R. G.: Hemophilia treated with spleen cells. J. Amer. med. Ass. 207, 1269 (1969).Google Scholar
  89. Des Prez, R. M., Horowitz, H. K., Hook, E. W.: Effects of bacterial endotoxin on rabbit platelets. I. Platelet aggregation and release of platelet factors in vitro. J. exp. Med. 114, 857 (1961).Google Scholar
  90. Deutsch, E., Schaden, W.: Zur Reinigung und Charakterisierung des VII. Blutgerinnungsfaktors. Biochem. Z. 324, 266 (1953).PubMedGoogle Scholar
  91. Deutsch, E., Irsigler, K., Lomoschitz, H.: Studien über Gewebethromboplastin. I. Reinigung, chemische Charakterisierung und Trennung in einen Eiweiß-und Lipoidanteil. Thrombos. Diathes. haemorrh. (Stuttg.) 12, 12 (1964).Google Scholar
  92. Deutsch, E., Lechner, K., Schmer, G.: On the purification of factor VII from bovine plasma. Thrombos. Diabthes. haemorrh. (Stuttg.), Suppl. 20, 275 (1966).Google Scholar
  93. De Vries, A., Alexander, B., Goldstein, R.: A factor in serum which accelerates the conversion of prothrombin to thrombin: I. Its determination and some physiologic and biochemical properties. Blood 4, 247 (1949).Google Scholar
  94. Dombrose, F. A., Seegers, W. H., Sedensky, J. A.: Antithrombin. Inhibition of thrombin and autoprothrombin C (F-Xa) as a mutual depletion system. Thrombos. Diathes. haemorrh. (Stuttg.) 26, 103 (1971).Google Scholar
  95. Donaldson, V. H.: Mechanisms of activation of C′1 esterase in hereditary angioneurotic edema plasma in vitro. J. exp. Med. 127, 411 (1968).PubMedGoogle Scholar
  96. Donaldson, V. H., Ratnoff, O. D.: Hageman factor alterations on physical properties during activation. Science 150, 754 (1965).PubMedGoogle Scholar
  97. Duckert, F., Flückiger, P., Koller, F.: Le role du facteur X dans la formation de la thromboplastine sanguine. Rev. Hémat. 9, 489 (1954).PubMedGoogle Scholar
  98. Duckert, F., Flückiger, P., Matter, M., Koller, F.: Clotting factor X. Physiologic and physico-chemical properties. Proc. Soc. exp. Biol. (N.Y.) 90, 17 (1955).PubMedGoogle Scholar
  99. Duckert, F., Jung, Y., Schmerling, D. H.: A hitherto undescribed congenital hemorrhagic diathesis, probably due to fibrin stabilizing factor deficiency. Thrombos. Diathes. haemorrh. (Stuttg.) 5, 179 (1961).Google Scholar
  100. Duckert, F., Koller, F., Matter, M.: Purification and physiological properties of factor VII from plasma and serum. Separation from prothrombin. Proc. Soc. exp. Biol. (N.Y.) 82, 259 (1953).PubMedGoogle Scholar
  101. Duckert, R.: The prephase accelerator. Present status. Thrombos. Diathes. haemorrh. (Stuttg.) 6, 254 (1961).Google Scholar
  102. Eagle, H.: Studies on blood coagulation. I. The role of prothrombin and of platelets in the formation of thrombin. J. gen. Physiol. 18, 531 (1935).PubMedGoogle Scholar
  103. Edman, P.: Method for determination of the amino acid sequence in peptides. Acta chem. scand. 4, 283 (1950).Google Scholar
  104. Egeberg, O.: A family with antihemophilic C factor (AHC = plasma thromboplastin antecedent) deficiency without bleeding tendency. Scand. J. clin. Lab. Invest. 14, 478 (1962).Google Scholar
  105. Egeberg, O.: Inherited antithrombin deficiency causing thrombophilia. Thrombos. Diathes. haemorrh. (Stuttg.) 13, 576 (1965a).Google Scholar
  106. Egeberg, O.: On the natural blood coagulation inhibitor system. Investigations of inhibitor factors based on antithrombin deficient blood. Thrombos. Diathes. haemorrh. (Stuttg.) 14, 473 (1965b).Google Scholar
  107. Egeberg, O.: Inherited fibrinogen abnormality causing thrombophilia. Thrombos. Diathes. haemorrh. (Stuttg.) 17, 176 (1967).Google Scholar
  108. Egeberg, O.: New families with hereditary hemorrhagic trait due to deficiency of fibrin stabilizing factor (fXIII). Thrombos. Diathes. haemorrh. (Stuttg.) 20, 534 (1968).Google Scholar
  109. Egeberg, O.: Factor XII defect and hemorrhage. Evidence for a new type of hereditary hemostatic disorder. Thrombos. Diathes. haemorrh. (Stuttg.) 23, 432 (1970).Google Scholar
  110. Eisen, V.: Fibrinolysis and the formation of biologically active polypeptides. Brit. med. Bull. 20, 205 (1964).PubMedGoogle Scholar
  111. Esnouf, M. P.: Plenary Session Papers, 12th Intern. Soc. Hematol., New York, 1968, p. 315.Google Scholar
  112. Esnouf, M. P., Jobin, F.: The isolation of factor V from bovine plasma. Biochem. J. 102, 660 (1967).PubMedGoogle Scholar
  113. Esnouf, M. P., Williams, W. J.: The isolation and purification of a bovine plasma protein which is a substrate for the coagulant fraction of Russell’s viper venom. Biochem. J. 84, 62 (1962).PubMedGoogle Scholar
  114. Evensen, S. A., Hjort, P. F.: Pathogenesis of disseminated intravascular coagulation. Plenary Session of XII. International Congr. of Hematology, 1970, p. 109.Google Scholar
  115. Evensen, S. A., Jeremic, M.: Intravascular coagulation with generalized Shwartzman reaction induced by Liquoid: lack of protection by extreme thrombocytopenia. Thrombos. Diathes. haemorrh. (Stuttg.) 19, 556 (1968).Google Scholar
  116. Evensen, S. A., Jeremic, M.: Platelets and the triggering of intravascular coagulation. Brit. J. Haemat. 19, 33 (1970).PubMedGoogle Scholar
  117. Evensen, S. A., Jeremic, M., Hjort, P. F.: Intravascular coagulation with generalized Shwartzman reaction induced by a heparin-like anticoagulant (Liquoid). Thrombos. Diathes. haemorrh. (Stuttg.) 18, 24 (1967).Google Scholar
  118. Fantl, P., Sawers, R. J.: Anticoagulant specificity and physiologically inactive betaprothromboplastin. Nature (Lond.) 177, 1233 (1956).PubMedGoogle Scholar
  119. Fantl, P., Sawers, R. J., Marr, A. G.: Investigation of a hemorrhagic disease due to beta-prothromboplastin deficiency complicated by a specific inhibitor of thromboplastin formation. Aust. Ann. Med. 5, 163 (1956).PubMedGoogle Scholar
  120. Feinstein, D. I., Chong, M. N. Y., Kasper, C. K., Rapaport, S. I.: Hemophilia A: Polymorphism detectable by a factor VIII antibody. Science 163, 1071 (1969).PubMedGoogle Scholar
  121. Fischer, Sh., Schwartz, M., Gottlieb, A., Ben Yoseph, N., Shapiro, S.: Fibrinolysis, fibrinogen and factor XIII in newborn infants. Thrombos. Diathes. haemorrh. (Stuttg.) 20, 542 (1968).Google Scholar
  122. Ganrot, P. O., Niléhn, J.-E.: Plasma prothrombin during treatment with dicumarol. II. Demonstration of an abnormal prothrombin fraction. Scand. J. clin. Lab. Invest. 22, 23 (1968).PubMedGoogle Scholar
  123. Ganrot, P. O., Niléhn, J. E.: Electrophoretic separation of two thrombin inhibitors in plasma and serum. Scand. J. clin. Lab. Invest. 24, 11 (1969).PubMedGoogle Scholar
  124. Gaston, L. W.: Studies on a family with elevated plasma level of factor V (proaccelerin) and a tendency to thrombosis. Pediatrics 68, 376 (1966).Google Scholar
  125. Gerhold, W. M., Tiongson, T., Mandel, E. E.: Studies of fibrin-stabilizing factor. Fed. Proc. 25, 446 (1966).Google Scholar
  126. Gladhaug, A., Prydz, H.: Purification of the coagulation factors VII and X from human serum. Some properties of factor VII. Biochim. biophys. Acta (Amst.) 215, 105 (1970).PubMedGoogle Scholar
  127. Glueck, H. I., Roehll, W., Jr.: Myocardial infarction in a patient with a Hageman (factor XII) defect. Ann. intern. Med. 64, 390 (1966).PubMedGoogle Scholar
  128. Gobbi, F.: The fractionation properties of human factor VIII. Thrombos. Diathes. haemorrh. (Stuttg.) 4, 253 (1960).Google Scholar
  129. Goodnight, S. H., Feinstein, D. I., Østerud, B., Rapaport, S. I.: Factor VII anti-bodyneutralizing material in hereditary and acquired factor VII deficiency. Blood 28, 1 (1971).Google Scholar
  130. Graham, J. B., Barrow, B. M., Hougie, S.: Stuart clotting defect. II. Genetic aspect of a “new” haemorrhagic state. J. clin. Invest. 36, 492 (1957).Google Scholar
  131. Graham, R. C., Jr., Ebert, R. H., Ratnoff, O. D., Moses, J. M.: Pathogenesis of inflammation. II. In vivo observations of the inflammatory effects of activated Hageman factor and bradykinin. J. exp. Med. 121, 807 (1965).PubMedGoogle Scholar
  132. Grammens, G. L., Prasad, A. S., Mammen, E. F., Barnhart, M. J.: Physico-chemical and immunological properties of bovine Hageman factor. Thrombos. Diathes. haemorrh. (Stuttg.) 25, 405 (1971).Google Scholar
  133. Gray, E. J., Schaefer, E. H., Jensen, H.: Studies on role of accelerator factor in blood clotting mechanism. Acta haemat. (Basel) 15, 314 (1956).PubMedGoogle Scholar
  134. Haanen, C., Hommes, F., Morselt, G.: Some observations on the role of Hageman factor in blood coagulation. Thrombos. Diathes. haemorrh. (Stuttg.) 6, 261 (1961).Google Scholar
  135. Haanen, C., Morselt, G., Schoenmakers, J.: Contact activation of Hageman factor and the interaction of Hageman factor and plasma thromboplastin antecedent. Thrombos. Diathes. haemorrh. (Stuttg.) 17, 307 (1967).Google Scholar
  136. Habermann, E.: In: Neue Aspekte der Trasylol-Therapie. Hrsg. R. Gross u. G. Kroneberg, S. 126. Stuttgart: Schattauer 1966.Google Scholar
  137. Hall, C. E., Slayter, H. S.: The fibrinogen molecule: its size, shape and mode of polymerization. J. biophys. biochem. Cytol. 5, 11 (1959).PubMedGoogle Scholar
  138. Hammarsten, O.: Über das Fibrinogen. Pflügers Arch. ges. Physiol. 19, 563 (1879).Google Scholar
  139. Hammarsten, O.: Weitere Beiträge zur Kenntnis der Fibrinbildung. Z. phys. Chem. 28, 98 (1899).Google Scholar
  140. Hardaway, R. M.: Syndromes of disseminated intravascular coagulation. With special reference to shock and hemorrhage, p. 484. Springfield: Charles C. Thomas 1966.Google Scholar
  141. Hardisty, R. M.: The reaction of blood coagulation factors with brain extracts. Brit. J. Haemat. 1, 323 (1955).PubMedGoogle Scholar
  142. Hardisty, R. M., Margolis, J.: The role of Hageman factor in the initiation of blood coagulation. Brit. J. Haemat. 5, 203 (1959).PubMedGoogle Scholar
  143. Harmison, C. R., Landaburu, R. H., Seegers, W. H.: Some physico-chemical properties of bovine thrombin. J. biol. Chem. 236, 1693 (1961).PubMedGoogle Scholar
  144. Harmison, C. R., Seegers, W. H.: Some physicochemical properties of bovine autoprothrombin. II. J. biol. Chem. 237, 3074 (1962).PubMedGoogle Scholar
  145. Hathaway, W. E., Alsever, J.: The relation of the Fletcher factor to factor XI and XII. Brit. J. Haemat. 18, 161 (1970).PubMedGoogle Scholar
  146. Hecht, E.: Lipids in blood clotting, Springfield, Ill.: Charles C. Thomas 1965.Google Scholar
  147. Hecht, E., Cho, M. G., Seegers, W. H.: Thromboplastin: nomenclature and preparation of protein-free material different from platelet factor 3 or lipid activator. Amer. J. Physiol. 193, 584 (1958).PubMedGoogle Scholar
  148. Hecht, E., Slotta, K. H.: The chemical nature of the lipid activator in blood coagulation. Amer. J. clin. Path. 37, 126 (1962).Google Scholar
  149. Hemker, H. C.: Preprothrombin (Complex?), a circulating anticoagulant in coumarin treated and vitamin K deficient patients. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 13, 380 (1964).Google Scholar
  150. Hemker, H. C., Esnouf, M. P., Hemker, P. W., Swart, A. C. W., Macfarlane, R. G.: Formation of prothrombin converting activity. Nature (Lond.) 215, 248 (1967).PubMedGoogle Scholar
  151. Hemker, H. C., Kahn, M. J. P.: Reaction sequence of blood coagulation. Nature (Lond.) 215, 1201 (1967).PubMedGoogle Scholar
  152. Hemker, H. C., Kahn, M. J. P., Devilee, P. P.: The adsorption of coagulation factors onto phospholipids. Its role in the reaction mechanism of blood coagulation Thrombos. Diathes. haemorrh. (Stuttg.) 24, 214 (1970).Google Scholar
  153. Hemker, H. C., Loeliger, E. A., Veltkamp, J. J., eds.: Human blood coagulation, p. 397. Boerhaave series. Leiden: Univ. Press 1969.Google Scholar
  154. Hemker, H. C., Muller, A. D.: Kinetic aspects of the interaction of blood clotting enzymes. VI. Localization of the site of blood-coagulation inhibitor by the protein induced by vitamin K absence (PIVKA). Thrombos. Diathes. haemorrh. (Stuttg.) 20, 78 (1968).Google Scholar
  155. Hemker, H. C., Veltkamp, J. J., Hensen, A., Loeliger, E. A.: On the nature of prothrombin biosynthesis. Nature (Lond.) 200, 589 (1963).PubMedGoogle Scholar
  156. Hemker, H. C., Veltkamp, J. J., Loeliger, E. A.: Kinetic aspects of the interaction of blood clotting enzymes. III. Demonstration of an inhibitor of prothrombin conversion in vitamin K deficiency. Thrombos. Diathes. haemorrh. (Stuttg.) 19, 346 (1968).Google Scholar
  157. Henschen, A.: Number and reactivity of disulfide bonds in fibrinogen and fibrin. Arkiv Kemi 22, 355 (1964).Google Scholar
  158. Henschen, A., Blombäck, B.: Amino acid composition of human and bovine fibrinogen and fibrin. Arkiv Kemi 23, 347 (1964).Google Scholar
  159. Hjort, P.: Intermediate reactions in the coagulation of blood with tissue thromboplastin, convertin, accelerin, prothrombinase, p. 183. Thesis. Olso: University Press 1957. Scand. J. clin. Lab. Invest. 9 (Suppl. 27), 183 (1957).Google Scholar
  160. Hjort, P., Rapaport, S. I., Owren, P. A.: Platelet accelerator: identical to proaccelerin and adsorbed from plasma? Scand. J. clin. Lab. Invest. 7, 97 (1955).PubMedGoogle Scholar
  161. Hoak, J. C., Swanson, L. W., Warner, E. D., Connor, W. E.: Myocardial infarction associated with severe factor XII deficiency. Lancet 1966 II, 884.Google Scholar
  162. Högenauer, E., Lechner, K., Deutsch, E.: Isolation and characterization of blood clotting factors VII and X. Thrombos. Diathes. haemorrh. (Stuttg.) 19, 304 (1968).Google Scholar
  163. Holemans, R., Roberts, H. R.: Hageman factor and in vivo activation of fibrinolysis. J. Lab. clin. Med. 64, 778 (1964).PubMedGoogle Scholar
  164. Holmsen, H., Day, H. J., Stormorken, H.: The blood platelet release reaction. Scand. J. Haemat. 6 (Suppl. 8), 1 (1969).Google Scholar
  165. Hopff, F.: Über die Hämophilie oder die erbliche Anlage zu tödlichen Blutungen. Inaugural-Dissertation Würzburg 1828. Quoted by Bulloch and Fildes, 1911.Google Scholar
  166. Horn, R. G., Collins, R. D.: Studies on the pathogenesis of the generalized Shwartzman reaction. The role of granulocytes. Lab. Invest. 18, 101 (1968).PubMedGoogle Scholar
  167. Hougie, C.: Effect of Russell’s viper venom (Stypven) on Stuart clotting defect. Proc. Soc. exp. Biol. (N.Y.) 93, 570 (1956).PubMedGoogle Scholar
  168. Hougie, C.: The role of factor V in the formation of blood thromboplastin. J. Lab. clin. Med. 50, 61 (1957).PubMedGoogle Scholar
  169. Hougie, C.: Reactions of Stuart factor and factor VII with brain and factor V. Proc. Soc. exp. Biol. (N.Y.) 101, 132 (1959).PubMedGoogle Scholar
  170. Hougie, C., Barrow, E. M., Graham, J. B.: Stuart clotting defect. I. Segregation of an hereditary hemorrhagic state from the heterogeneous group heretofore called “stable factor” (SPCA, proconvertin, factor VII) deficiency. J. clin. Invest. 36, 485 (1957).PubMedGoogle Scholar
  171. Hougie, C., Denson, K. W. E., Biggs, R.: A study of the reaction product of factor VIII and factor IX by gel filtration. Thrombos. Diathes. haemorrh. (Stuttg.) 18, 211 (1967).Google Scholar
  172. Hougie, C., Twomey, J. J.: Hemophilia Bm. A new type of factor IX deficiency. Lancet 1967 I, 698.Google Scholar
  173. Howell, W. H.: The nature and action of the thromboplastic (zymoplastic) substance of the tissues. Amer. J. Physiol. 31, 1 (1912).Google Scholar
  174. Howell, W. H.: The coagulation of blood. Harvey Lect. 12, 272 (1916–1917).Google Scholar
  175. Hoyer, L. W., Breckenridge, R. T.: Immunologic studies of antihemophilic factor (AHF, factor VIII).: Cross-reacting material in a genetic variant of hemophilia A. Blood 32, 962 (1968).PubMedGoogle Scholar
  176. Huseby, R. M., Murray, M.: Molecular structure of fibrinogen. I. Helical content and the role of the tyrosine moiety in the fibrinogen molecule. Biochim. biophys. Acta (Amst.) 133, 243 (1967a).PubMedGoogle Scholar
  177. Huseby, R. M., Murray, M.: The circular dichroism and optical rotatory dispersion of fibrinogen: states of the aromatic amino acid residues in the molecule. Fed. Proc. 26, 537 (1967b).Google Scholar
  178. Hussain, Q. Z., Newcomb, T. F.: Effects of thrombin on factor V. Ann. Biochem. exp. Med. 23, 569 (1963).PubMedGoogle Scholar
  179. Huth, K., Löffler, H., Lechelmayr, U.: Verbrauchskoagulopathie bei unreifzelligen Leukosen. Verh. dtsch. Ges. inn. Med. 74, 147 (1968).PubMedGoogle Scholar
  180. Hvatum, N., Prydz, H.: Studies on tissue thromboplastin. Its splitting into two separable parts. Thrombos. Diathes. haemorrh. (Stuttg.) 21, 217 (1969).Google Scholar
  181. Iatridis, S. G., Ferguson, J. H.: Effect of surface and Hageman factor on the endogenous or spontaneous activation of the fibrinolytic system. Thrombos. Diathes. haemorrh. (Stuttg.) 6, 411 (1961).Google Scholar
  182. Iatridis, S. G., Ferguson, J. H.: Active Hageman factor: A plasma lysokinase of the human fibrinolytic system. J. clin. Invest. 41, 1277 (1962).PubMedGoogle Scholar
  183. Ingram, C. Y. C., McBrien, D. J., Spencer, H.: Fatal pulmonary embolism in congenital fibrinogenopenia. Acta haemat. (Basel) 35, 36 (1966).Google Scholar
  184. Izak, G., Galewsky, K.: Studies on experimentally induced hypercoagulable state in rabbits. Thrombos. Diathes. haemorrh. (Stuttg.) 16, 228 (1966).Google Scholar
  185. Jackson, C. M., Hanahan, D. J.: Studies on bovine factor X. II. Characterization of purified factor X. Observations on some alterations in zone electrophoretic and chromatographic behavior occurring during purification. Biochemistry 7, 4506 (1968).PubMedGoogle Scholar
  186. Jackson, C. M., Johnson, T. F., Hanahan, D. J.: Studies on bovine factor X. I. Large scale purification of the bovine plasma protein possessing factor X activity. Biochemistry 7, 4492 (1968).PubMedGoogle Scholar
  187. Jackson, D. P., Beck, E. A., Charache, P.: Congenital disorders of fibrinogen. Fed. Proc. 24, 816 (1965).PubMedGoogle Scholar
  188. Jaques, L. B., Fidlar, E., Feldsted, E. T., Macdonald, A. G.: Silicones and blood coagulation. Canad. med. Ass. J. 55, 26 (1946).Google Scholar
  189. Jensen, H., Gray, E. J., Schaefer, E. H.: Formation of blood thrombokinase. Acta haemat. (Basel) 13, 377 (1955).PubMedGoogle Scholar
  190. Jobin, F., Esnouf, M. P.: Studies on the formation of the prothrombin converting complex. Biochem. J. 102, 666 (1967).PubMedGoogle Scholar
  191. Johnson, A. J., Newman, J., Howell, M. B., Puszkin, S.: Purification of antihemophilic factor (AHF) for clinical and experimental use. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 26, 377 (1967).Google Scholar
  192. Johnson, P., Mihalyi, E.: Physicochemical studies of bovine fibrinogen. I. Molecular weight and hydrodynamic properties of fibrinogen and fibrinogen cleaned by sulfite in 5 M guanidine-HCl solution. Biochim. biophys. Acta (Amst.) 102, 467 (1965).PubMedGoogle Scholar
  193. Johnson, S. A., Seegers, W. H.: Studies on the plasma defect in hemophilia. Rev. Hémat. 9, 529 (1954).PubMedGoogle Scholar
  194. Jorpes, J. E.: One hundred years of research on blood coagulation leading to the present day anticoagulant therapy in thrombosis. Thrombosis and Embolism, I. International Conference, Basel, 1954, p. 23–30. Basel: Benno Schwabe & Co. 1954.Google Scholar
  195. Josso, F., Lavergne, J. M., Gouault, M., Prou-Wartelle, O., Soulier, J. P.: Differents états moleculaires du facteur II (prothrombine). Leur étude à l’aide de la staphylocoagulase et traités par les antagonistes de la vitamine K. Thrombos. Diathes. haemorrh. (Stuttg.) 20, 88 (1968).Google Scholar
  196. Josso, F., Prou-Wartelle, O.: Interaction of tissue factor and factor VII at the earliest phase of coagulation. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 17, 45 (1965).Google Scholar
  197. Jürgens, J.: The significance of the Hageman-factor for the effect of wettable surface on thrombocytes. Thrombos. Diathes. haemorrh. (Stuttg.) 7, 48 (1962).Google Scholar
  198. Kahn, M. J. P., Bourgain, R. H.: A simplified preparation procedure of factor X by paper electrophoresis. Hemostase 5, 413 (1965).PubMedGoogle Scholar
  199. Kahn, M. J. P., Hemker, H. C.: Studies on blood coagulation factor V. I. The interaction of salts of fatty acids and coagulation factors. Thrombos. Diathes. haemorrh. (Stuttg.) 222, 417 (1969).Google Scholar
  200. Kahn, M. J. P., Hemker, H. C.: Studies on blood coagulation factor V. V. Changes of molecular weight accompanying activation of factor V by thrombin and the procoagulant protein of Russell’s viper venom. Thrombos. Diathes. haemorrh. (Stuttg.) 27, 25 (1972).Google Scholar
  201. Kattlove, H. E., Shapiro, S. S., Spivack, M.: Hereditary prothrombin deficiency. New Engl. J. Med. 282, 57 (1970).PubMedGoogle Scholar
  202. Kekwick, R. A., Mackay, M. E., Nance, M. H., Record, B. R.: The purification of human fibrinogen. Biochem. J. 60, 671 (1955).PubMedGoogle Scholar
  203. Kellermeyer, R. W., Breckenridge, R. T.: The inflammatory process in acute gouty arthritis. I. Activation of Hageman factor by sodium urate crystals. J. Lab. clin. Med. 65, 307 (1965).PubMedGoogle Scholar
  204. Kellermeyer, R. W., Graham, R. C.: Kinins—possible physiologic and pathologic roles in man. New Engl. J. Med. 249, 754 (1968).Google Scholar
  205. Kezdy, F. J., Lorand, L., Miller, K. D.: Titration of active centers in thrombin solutions. Standardization of the enzyme. Biochemistry 157, 2302 (1965).Google Scholar
  206. Kingdon, H. S., Davie, E. W., Ratnoff, O. D.: The reaction between activated plasma thromboplastin antecedent and diisopropylphosphofluoridate. Biochemistry 3, 166 (1964).PubMedGoogle Scholar
  207. Kjærheim, A., Hovig, T.: The ultrastructure of haemostatic blood platelet plugs in rat mesenterium. Thrombos. Diathes. haemorrh. (Stuttg.) 7, 1 (1962).Google Scholar
  208. Koller, F., Krüsi, G., Luchsinger, P.: Über eine besondere Form haemorrhagischer Diathese. Schweiz. med. Wschr. 80, 1101 (1950).PubMedGoogle Scholar
  209. Koller, F., Loeliger, A., Duckert, F.: Experiments on a new clotting factor (factor VII). Acta haemat. (Basel) 6, 1 (1951).PubMedGoogle Scholar
  210. Koller, F., Loeliger, A., Duckert, F.: Le facteur VII. Rev. Hémat. 7, 156 (1952).PubMedGoogle Scholar
  211. Korsan-Bengtsen, K., Hjort, P. F., Ygge, J.: Acquired factor X deficiency in a patient with amyloidosis. Thrombos. Diathes. haemorrh. (Stuttg.) 7, 558 (1962).Google Scholar
  212. Korsan-Bengtsen, K., Ygge, J.: Purification of human thrombin on a carboxymethyl-cellulose column. Scand. J. Lab. clin. Invest. 13, 591 (1961).Google Scholar
  213. Kowalski, E.: Fibrinogen derived inhibitors of blood coagulation. Thrombos. Diathes. haemorrh. (Stuttg.) 4, Suppl. Blood Clotting factors, 211 (1959).Google Scholar
  214. Laki, K., Lorand, L.: On the solubility of fibrin clots. Science 108, 280 (1948).PubMedGoogle Scholar
  215. Lamy, F., Waugh, D. F.: The physical changes of prothrombin under various experimental conditions. Thrombos. Diathes. haemorrh. (Stuttg.) 2, 12 (1958).Google Scholar
  216. Lanchantin, G. F., Friedman, J. A.: Isolation of human plasma prothrombin of high specific activity by gel giltration. Proc. Soc. exp. Biol. (N.Y.) 114, 584 (1963).PubMedGoogle Scholar
  217. Lanchantin, G. F., Hart, D. W., Friedman, J. A., Saavedra, N. V., Mehl, J. W.: Amino acid composition of human plasma prothrombin. J. biol. Chem. 243, 5379 (1968).Google Scholar
  218. Larrieu, M. J., Meyer, D.: Abnormal factor IX during anticoagulant treatment. Lancet 1970 II, 1085.Google Scholar
  219. Larrieu, M. J., Meyer, D.: Heterogeneity of factor VIII and factor IX variants. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 43, 11 (1971).Google Scholar
  220. Lasch, H. G., Heene, D. L., Huth, K., Sandritter, W.: Pathophysiology, clinical manifestations and therapy of consumption-coagulopathy (“Verbrauchskoagulopathie”). Amer. J. Cardiol. 20, 381 (1967).PubMedGoogle Scholar
  221. Lechner, K.: In: Hämophilie. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 37, 79 (1969).Google Scholar
  222. Lechner, K., Deutsch, E.: Activation of factor X. Thrombos. Diathes. haemorrh. (Stuttg.) 13, 314 (1965).Google Scholar
  223. Lechner, L.: Immune reactive factor IX in acquired factor IX deficiency. Thrombos. Diathes. haemorrh. (Stuttg.) 27, 19 (1972).Google Scholar
  224. Lewis, J. H.: Synthesis of AHF in von Willebrand’s disease. Blood 23, 233 (1964).PubMedGoogle Scholar
  225. Lewis, J. H., Merchant, W. R.: The probable identity of glass factor with Hageman factor. J. clin. Invest. 37, 911 (1958).Google Scholar
  226. Lewis, J. H., Walters, D., Didisheim, P., Merchant, W. R.: Application of continuous flow electrophoresis to the study of the blood coagulation proteins and fibrinolytic enzyme system. I. Normal human materials. J. clin. Invest. 37, 1323 (1958).PubMedGoogle Scholar
  227. Lewis, M. L., Ware, A. G.: A simple procedure for separation of prothrombin and accelerator globulin from citrated human plasma. Proc. Soc. exp. Biol. (N.Y.) 84, 636 (1953).PubMedGoogle Scholar
  228. Lipinski, B., Worowski, K., Jeljaszewicz, J., Niewiarowski, S., Rejniak, L.: Participation of soluble fibrin monomer complexes and platelet factor 4 in the generalized Shwartzman reaction. Thrombos. Diathes. haemorrh. (Stuttg.) 20, 285 (1968).Google Scholar
  229. Lister, J.: Croonian lecture: on the coagulation of the blood. Proc. roy. Soc. 12, 580 (1863).Google Scholar
  230. Liston, R.: Haemorrhagic idiosyncrasy. Lancet 1839 II, 137.Google Scholar
  231. Loeliger, E. A., Hers, J. F. P.: Chronic antithrombinaemia (antithrombin V) with hemorrhagic diathesis in a case of rheumatoid arthritis with hypergammaglobulinaemia. Thrombos, Diathes. haemorrh. (Stuttg.) 1, 499 (1957).Google Scholar
  232. Loewy, A. G., Dahlberg, J. E., Dorwart, W. V., Weber, M., Eisele, J.: A transamidase mechanism for insoluble fibrin formation. Biochem. biophys. Res. Commun. 15, 77 (1964).Google Scholar
  233. Loewy, A. G., Dunathan, K., Kriel, R., Wolfinger, H. L.: Fibrinase. I. Purification of substrate and enzyme. J. biol. Chem. 236, 2625 (1961a).PubMedGoogle Scholar
  234. Lorand, L.: “Fibrinopeptide“. New aspects of the fibrinogen-fibrin transformation. Nature (Lond.) 167, 992 (1951).PubMedGoogle Scholar
  235. Lorand, L.: Fibrino-peptide. Biochem. J. 52, 200 (1952).PubMedGoogle Scholar
  236. Lorand, L., Downey, J., Gotoh, T., Jacobsen, A., Tokura, S.: The transpeptidase system which crosslinks fibrin by γ-glutamyl-ε-lysine bonds. Biochem. biophys. Res. Commun. 31, 222 (1968).PubMedGoogle Scholar
  237. Lorand, L., Jacobsen, C. A.: Studies on the polymerisation of fibrin. The role of the globulin: Fibrin-stabilizing factor. J. biol. Chem. 230, 401 (1958).Google Scholar
  238. Lorand, L., Konishi, K.: Activation of fibrin-stabilizing factor of plasma by thrombin. Arch. Biochem. 105, 58 (1964).PubMedGoogle Scholar
  239. Lorand, L., Konishi, K.: Separation of activated fibrin-stabilizing factor from thrombin. Biochim. biophys. Acta (Amst.) 121, 177 (1966).PubMedGoogle Scholar
  240. Lorand, L., Konishi, K., Jacobsen, A.: Transpeptidation mechanism in blood clotting. Nature (Lond.) 194, 1148 (1962).PubMedGoogle Scholar
  241. Lüscher, E. F.: Kontaktivierung, biologisch gesehen. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 25, 79 (1968).Google Scholar
  242. Lyttleton, J. W.: The antithrombin activity of human plasma. Biochem. J. 58, 8 (1954).PubMedGoogle Scholar
  243. Macfarlane, R. G.: The coagulant action of Russell’s viper venom. The use of antivenom in defining its reaction with a serum factor. Brit. J. Haemat. 7, 496 (1961).PubMedGoogle Scholar
  244. Macfarlane, R. G.: In: Metabolism and physiological significance of lipids (R. M. C. Dawson and D. N. Rhodes, eds.), p. 325–335. London-New York 1964.Google Scholar
  245. Macfarlane, R. G.: An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier. Nature (Lond.) 202, 495 (1964).Google Scholar
  246. Macfarlane, R. G., Biggs, R., Ash, B. J., Denson, K. W. E.: The activation and consumption of factor X in recalcified plasma. The effect of added factor VIII and Russell’s viper venom. Brit. J. Haemat. 10, 530 (1964).PubMedGoogle Scholar
  247. Magnusson, S.: NH2-terminal amino acid residues in bovine prothrombin and in prothrombin activation mixtures. With a note on the amino acid composition of chromatographically purified bovine prothrombin. Arkiv Kemi 23, 271 (1965a).Google Scholar
  248. Magnusson, S.: Preparation and carbohydrate analysis of bovine prothrombin. Arkiv Kemi 23, 285 (1965b).Google Scholar
  249. Magnusson, S.: Fractionation of bovine prothrombin preparations by gradient chromatography on DEAE-cellulose columns. Arkiv Kemi 24, 217 (1965c).Google Scholar
  250. Magnusson, S.: Preparation of highly purified bovine thrombin (E.C. and determination of its N-terminal amino acid residues. Arkiv Kemi 24, 349 (1965d).Google Scholar
  251. Magnusson, S.: Purification of prothrombin from human citrated plasma fraction II + III (Cohn’s method). Arkiv Kemi 24, 367 (1965e).Google Scholar
  252. Magnusson, S.: Edman degradation of components of the bovine and human prothrombin-thrombin systems. Arkiv Kemi 24, 375 (1965f).Google Scholar
  253. Magnusson, S.: On the structure of thrombin and prothrombin. In: Human blood coagulation, ed. Hemker et al., p. 18. Leiden: University Press 1969.Google Scholar
  254. Mammen, E. F.: Mechanism of factor VIII inactivation. Fed. Proc. 24, 452 (1965).Google Scholar
  255. Mammen, E. F.: Physiology and biochemistry of blood coagulation. In: Thrombosis and bleeding disorders, p. 554, ed. Bang et al. New York: Academic Press 1971.Google Scholar
  256. Mammen, E. F., Ramien, A.: Die Anwendung der Gelfiltration zur weiteren Reinigung von Rinder-Prothrombin. Thrombos. Diathes. haemorrh. (Stuttg.) 8, 37 (1962).Google Scholar
  257. Mammen, E. F., Thomas, W. R., Seegers, W. H.: Activation of purified prothrombin to autoprothrombin I or autoprothrombin II (platelet cofactor II) or autoprothrombin II-A. Thrombos. Diathes. haemorrh. (Stuttg.) 5, 218 (1960a).Google Scholar
  258. Mammen, E. F., Yoshinari, M., Seegers, W. H.: Platelet cofactors as plasma components of the intrinsic blood clotting mechanism. Thrombos. Diathes. haemorrh. (Stuttg.) 5, 38 (1960b).Google Scholar
  259. Marciniak, E., Seegers, W. H.: Prethrombin as a new sub-unit of prothrombin. Nature (Lond.) 209, 621 (1966).PubMedGoogle Scholar
  260. Marcus, A. J., Ullman, H. L., Safier, L. B., Ballard, H. S.: Platelet phosphatids. Their fatty acid and aldehyd composition and activity in different clotting systems. J. clin. Invest. 41, 2198 (1962).PubMedGoogle Scholar
  261. Margaretten, W., Zunker, H. O., McKay, D. G.: Production of the generalized Shwartzman reaction in pregnant rats by intravenous infusion of thrombin. Lab. Invest. 13, 552 (1964).PubMedGoogle Scholar
  262. Margolis, J.: Initiation of blood coagulation by glass and related surfaces. J. Physiol. (Lond.) 137, 95 (1957).PubMedGoogle Scholar
  263. Margolis, J.: Activation of plasma by contact with glass. Evidence for a common reaction which releases plasma kinin and initiates coagulation. J. Physiol. (Lond.) 144, 1 (1958a).PubMedGoogle Scholar
  264. Margolis, J.: Activation of permeability factor in plasma by contact with glass. Nature (Lond.) 181, 635 (1958b).PubMedGoogle Scholar
  265. Margolis, J.: The role of Hageman factor in plasma/surface reactions. In: Hemophilia and other hemorrhagic states (K. M. Brinkhous, ed.), p. 208. Chapel Hill: University of North Carolina Press 1959.Google Scholar
  266. Margolis, J.: The mode of action of Hageman factor in the release of plasma kinin. J. Physiol. (Lond.) 151, 238 (1960).PubMedGoogle Scholar
  267. Margolis, J.: The interrelationship of coagulation plasma and release of peptides. Ann. N.Y. Acad. Sci. 104, 133 (1963).PubMedGoogle Scholar
  268. Matacic, S., Loewy, A. G.: The identification of isopeptide crosslinks in insoluble fibrin. Biochem. biophys. Res. Commun. 30, 356 (1968.PubMedGoogle Scholar
  269. McGrath, J. M., Stewart, G. J.: The effects of endotoxin on vascular endothelium. J. exp. Med. 129, 833 (1969).PubMedGoogle Scholar
  270. McKay, D. G.: Disseminated intravascular coagulation: and intermediary mechanism of disease, p. 493. New York: Harper Row publ. 1965.Google Scholar
  271. Mellanby, J.: The coagulation of the blood. J. Physiol. (Lond.) 38, 28, 441 (1909).Google Scholar
  272. Ménaché, D.: Constitutional and familial abnormal fibrinogen. In: Fibrinogen and fibrin. Turnover of clotting factors. Ed. Hunter et al. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 13, 193 (1964).Google Scholar
  273. Ménaché, D.: Congenitally abnormal fibrinogens. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 39, 307 (1970).Google Scholar
  274. Ménaché, D., Boivin, P.: Deficit acquis en facteur X chez une malade atteint d’amyloidose primitive: injection d’un fraction CSB. Nouv. Rev. franç. Hémat. 2, 868 (1962).Google Scholar
  275. Meyer, D., Lavergne, J.-M., Larrieu, M.-J., Josso, F.: Cross-reacting material in congenital factor VIII deficiencies. (Haemophilia A and von Willebrand’s disease), p. 183. New York: Pergamon Press Inc. 1972.Google Scholar
  276. Miller, L. L., Hanavan, H. R., Titthasiri, N., Chowdhury, A.: Dominant role of the liver in the biosynthesis of the plasma proteins with special reference to the plasma mucoproteins (seromucoid) ceruloplasmin and fibrinogen. Chemistry 44, 17 (1964).Google Scholar
  277. Miller, L. L. John, D. W.: Factors affecting the net fibrinogen biosynthesis by the isolated perfused rat liver. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 34, 127 (1970).Google Scholar
  278. Miller, S. P.: Coagulation dynamics in factor V deficiency: A family study with a note on the occurrence of thrombophlebitis. Thrombos. Diathes. haemorrh. (Stuttg.) 13, 500 (1965).Google Scholar
  279. Miller, S. P., Siggerud, J.: Abnormal blood coagulation in carriers of haemophilia. J. Lab. clin. Med. 63, 601 (1964).Google Scholar
  280. Monkhouse, F. C., France, E. S., Seegers, H. W.: Studies on the antithrombin and heparin cofactor activities of a fraction adsorbed from plasma by aluminium hydroxide. Circulat. Res. 3, 397 (1955).PubMedGoogle Scholar
  281. Morawitz, P.: Beiträge zur Kenntnis der Blutgerinnung. Arch. klin. Med. 79, 215 (1904).Google Scholar
  282. Morawitz, P.: Die Chemie der Blutgerinnung. Ergebn. Physiol. 4, 307 (1905).Google Scholar
  283. Mosesson, M. W.: Molecular heterogeneity of human fibrinogen. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 34, 63 (1970).Google Scholar
  284. Mosesson, M. W., Alkjaersig, N., Sweet, B., Sherry, S.: Human fibrinogen of relatively high solubility. Comparative biophysical, biochemical, and biological studies with fibrinogen of lower solubility. Biochemistry 6, 3279 (1967).PubMedGoogle Scholar
  285. Mosesson, M. W., Sherry, S.: The preparation and properties of human fibrinogen of relatively high solubility. Biochemistry 5, 2829 (1966).PubMedGoogle Scholar
  286. Müller-Berghaus, G., Lasch, H.-G.: Untersuchungen über Beziehungen zwischen Gefäß-und Gerinnungsfaktoren beim Sanarelli-Shwartzman-Phänomen. Thrombos. Diathes. haemorrh. (Stuttg.) 9, 335 (1963).Google Scholar
  287. Müller-Berghaus, G., Lasch, H. G.: Consumption of Hageman factor activity in the generalized Shwartzman reaction induced by Liquoid. Its prevention by inhibition of Hageman factor activation. Thrombos. Diathes. haemorrh. (Stuttg.) 23, 386 (1970).Google Scholar
  288. Müller-Berghaus, G., Lasch, H. G.: Hageman factor activity in liquoid-induced consumption coagulopathy. Thrombos. Diathes. haemorrh. (Stuttg.) 26, 38 (1971).Google Scholar
  289. Muirhead, C. R., Triantaphyllopoulos, D. C.: Anticoagulants produced by thrombin from fibrin, the effect on blood coagulation, some physical characteristics. Thrombos. Diathes. haemorrh. (Stuttg.) 26, 211 (1971).Google Scholar
  290. Murano, G.: Some biochemical aspects of the prothrombin complex. Ph.D. Dissertation, Wayne State University, Detroit 1968.Google Scholar
  291. Murano, G.: Purification of thrombin. In: Thrombosis and bleeding disorders, ed. Bang et al., p. 124. New York: Acad. Press 1971.Google Scholar
  292. Murray, M.: Vasculokinase, a clotting substance from arteries. Amer. J. clin. Path. 36, 500 (1961).Google Scholar
  293. Mustard, J. F., Medway, W., Downie, H. G., Roswell, H. C.: Effects of intravenous phospholipid containing phosphatidyl serine on blood clotting with particular reference to the Russell’s viper venom time. Nature (Lond.) 196, 1063 (1962).PubMedGoogle Scholar
  294. Nemerson, Y.: The reaction between bovine brain tissue factor and factors VII and X. Biochemistry 5, 601 (1966).PubMedGoogle Scholar
  295. Nemerson, Y., Spaet, T. H.: The activation of factor X by extracts of rabbit brain. Blood 23, 657 (1964).PubMedGoogle Scholar
  296. Newman, J., Johnson, A. J., Karpatkin, M. H., Puszkin, S.: Methods for the production of clinically effective intermediate and high purity factor VIII concentrates. Brit. J. Haemat. 21, 1 (1971).PubMedGoogle Scholar
  297. Niemetz, J., Nossel, H. L.: Method of purification and properties of anti-XIa inhibitor of contact product. Thrombos. Diathes. haemorrh. (Stuttg.) 17, 335 (1967).Google Scholar
  298. Niewiarowski, S., Bankowski, E., Fiedoruk, T.: Adsorption of Hageman factor (factor XII) on collagen. Experientia (Basel) 20, 367 (1964).PubMedGoogle Scholar
  299. Niewiarowski, S., Bankowski, E., Rogowicka, I.: Studies on the adsorption and activation of the Hageman factor (factor XII) by collagen and elastin. Thrombos. Diathes. haemorrh. (Stuttg.) 14, 387 (1965).Google Scholar
  300. Niewiarowski, S., Kowalski, E.: Formation of an antithrombin-like anticoagulant during proteolysis of fibrinogen. Bull. Acad. pol. Sci. Cl. 2 5, 169 (1957).Google Scholar
  301. Niewiarowski, S., Kowalski, E.: Une nouvel anticoagulant dérivé du fibrinogene. Rev. Hémat. 13, 320 (1958).PubMedGoogle Scholar
  302. Niewiarowski, S., Prou-Wartelle, O.: Role du facteur contact (Facteur Hageman) dans la fibrinolyse. Thrombos. Diathes. haemorrh. (Stuttg.) 3, 593 (1959).Google Scholar
  303. Niewiarowski, S., Stachurska, J., Wegrzynowicz, Z.: Arginine esterase activity of the contact (Hageman) factor. Thrombos. Diathes. haemorrh. (Stuttg.) 7, 514 (1962).Google Scholar
  304. Nilsson, I. M., Blombäck, M.: Von Willebrand’s disease in Sweden. Its pathogenesis and treatment. Acta med. scand. 164, 263 (1959).PubMedGoogle Scholar
  305. Nilsson, I. M., Blombäck, M.: Von Willebrand’s disease in Sweden—occurrence, pathogenesis and treatment. Thrombos. Diathes. haemorrh. (Stuttg.) 9, Suppl. 11, 103 (1963).Google Scholar
  306. Nilsson, I. M., Blombäck, M., Jorpes, E., Blombäck, B., Johansson, S. A.: Von Willebrand’s disease and its correction with human plasma fraction 1-0. Acta med. scand. 159, 179 (1957).PubMedGoogle Scholar
  307. Nilsson, I. M., Thielen, A., von Franckeu, I.: Carriers of haemophilia A. A laboratory study. Acta med. scand. 165, 357 (1959).PubMedGoogle Scholar
  308. Norman, J. C., Covelli, V. H., Sise, H. S.: Transplantation of the spleen: Experimental cure of hemophilia. Surgery 64, 1 (1968).PubMedGoogle Scholar
  309. Nossel, H. L.: The contact phase of blood coagulation, p. 176. Oxford: Blackwell Scientific Publication 1964.Google Scholar
  310. Nossel, H. L.: Differential consumption of coagulation factors resulting from activation of the extrinsic (tissue thromboplastin) or the intrinsic (foreign surface contact) pathways. Blood 29, 331 (1967).PubMedGoogle Scholar
  311. Nossel, H. L.: The earliest stages of blood coagulation. In: Recent advances in blood coagulation, ed. Poller, p. 39. London: J. A. Churchill 1969.Google Scholar
  312. Nossel, H. L., Niemetz, J.: A normal inhibitor of the blood coagulation contact reaction product. Blood 25, 712 (1965).PubMedGoogle Scholar
  313. Nossel, H. L., Rubin, H., Drillings, M., Hsieh, R.: Inhibition of Hageman factor activation. J. clin. Invest. 47, 1172 (1968).PubMedGoogle Scholar
  314. Nussbaum, M., Morse, B. S.: Plasma fibrin stabilizing factor activity in various diseases. Blood 23, 669 (1964).PubMedGoogle Scholar
  315. O’Brien, J. R.: The effect of some fatty acids and phospholipids on blood coagulation. Brit. J. exp. Path. 38, 529 (1957).PubMedGoogle Scholar
  316. Østerud, B., Berre, Å., Otnaess, A. B., Björklid, A., Prydz, H.: Activation of the coagulation factor VII by tissue thromboplastin and Calcium. Biochemistry 11, 2853 (1972).PubMedGoogle Scholar
  317. Øzge-Anwar, A. H., Movat, H. Z., Scott, J. G.: The kinin system of human plasma. IV. The interrelationship between the contact phase of blood coagulation and the plasma kinin system in man. Thrombos. Diathes. haemorrh. (Stuttg.) 27, 139 (1972).Google Scholar
  318. Ogston, D., Bennett, N. B., Ogston, C. M., Ratnoff, O. D.: The assay of a plasma component necessary for the generation of a plasminogen activator in the presence of Hageman factor (Hageman factor co-factor). Brit. J. Haemat. 20, 209 (1971).PubMedGoogle Scholar
  319. Ottaviani, P. F., Mándelli, F., Fontana, L., Morelli, R.: Comportomento del fattore stabilizzante fibrinico nelle epatopatie. Progr. Med. 21, 115 (1965).Google Scholar
  320. Owen, C. A., Bollman, J. L.: Prothrombin conversion factor of dicoumarol plasma. Proc. Soc. exp. Biol. (N.Y.) 67, 231 (1948).PubMedGoogle Scholar
  321. Owen, C. A., Magath, T. B., Bollman, J. L.: Prothrombin conversion factors in blood coagulation. Amer. J. Physiol. 166, 1 (1951).PubMedGoogle Scholar
  322. Owren, P. A.: Nye undersøkelser over blodets koagulasjon. Proc. Norwegian Acad. of Science p. 21 (1944).Google Scholar
  323. Owren, P. A.: The coagulation of blood, investigations on a new clotting factor. Acta med. scand. 128 (Suppl. 194), 327 (1947a).Google Scholar
  324. Owren, P. A.: The fifth coagulation factor (factor V). Preparation and properties. Biochem. J. 43, 136 (1948).Google Scholar
  325. Owren, P. A.: New factors concerned in the coagulation of blood. Bull. Acad. Suisse Sci. Med. 3, 163 (1947/48b).Google Scholar
  326. Owren, P. A.: The diagnostic and prognostic significance of plasma prothrombin and factor V levels in parenchymatous hepatitis and obstructive jaundice. Scand. J. clin. Lab. Invest. 1, 131 (1949).Google Scholar
  327. Owren, P. A.: The diagnosis of the hemophilic conductor. Proc. Int. Soc. Haemat. 1950. Paper no. 104 A.Google Scholar
  328. Owren, P. A.: Proconvertin—the new clotting factor. Scand. J. clin. Lab. Invest. 3, 168 (1951).Google Scholar
  329. Owren, P. A.: New clotting factors. In: Blood clotting and allied problems. 5th Conference, p. 92. New York: Josiah Macy Foundation 1952a.Google Scholar
  330. Owren, P. A.: La proconvertine. Rev. Hémat. 7, 147 (1952b).PubMedGoogle Scholar
  331. Owren, P. A.: Prothrombin and accessory factors. Clinical significance. Amer. J. Med. 14, 201 (1953).PubMedGoogle Scholar
  332. Owren, P. A.: Thrombotest. A new method for controlling anticoagulant therapy. Lancet 1959 II, 774.Google Scholar
  333. Owren, P. A.: Critical study of tests for control of anticoagulant therapy. Thrombos. Diathes. (haemorrh.) Stuttg.) 7, Suppl. 1, 294 (1962).Google Scholar
  334. Owren, P. A.: Control of anticoagulant therapy. The use of new tests. Arch. intern. Med. 3, 248 (1963).Google Scholar
  335. Owren, P. A.: Recent advances in the control of anticoagulant therapy. Geriatrics 26, 74 (1971).PubMedGoogle Scholar
  336. Papahadjopoulos, D., Hougie, C., Hanahan, D. J.: Influence of surface charge of phospholipids on their clot-promoting activity. Proc. Soc. exp. Biol. (N.Y.) 111, 412 (1962).Google Scholar
  337. Papahadjopoulos, D., Hougie, C., Hanahan, D. J.: Purification of bovine factor V: a change of molecular size during blood coagulation. Biochemistry 3, 264 (1964).PubMedGoogle Scholar
  338. Papahadjopoulos, D., Yin, E. T., Hanahan, D. J.: Purification and properties of bovine factor X. Molecular changes during activation. Biochemistry 3, 1931 (1964).PubMedGoogle Scholar
  339. Pascuzzi, C. A., Spittel, J. A., Thompson, J. H., Owen, C. A.: Thromboplastin generation accelerator, a newly recognized component of the blood coagulation mechanism present in excess in certain thrombotic states. J. clin. Invest. 40, 1006 (1961).PubMedGoogle Scholar
  340. Patek, A. J., Taylor, F. H. L.: Hempohilia. II. Some properties of a substance obtained from normal human plasma effective in accelerating the coagulation of hemophilic blood. J. clin. Invest. 16, 113 (1937).PubMedGoogle Scholar
  341. Pavlovsky, A.: Contribution to the pathogenesis of hemophilia. Blood 2, 185 (1947).PubMedGoogle Scholar
  342. Pechet, L., Cochios, F., Deykin, D.: Further studies on the “Dynia” clotting abnormality. Thrombos. Diathes. haemorrh. (Stuttg.) 17, 365 (1967).Google Scholar
  343. Pechet, L., Kastrul, J. J.: Amyloidosis associated with factor X (Stuart) deficiency. Case report. Ann. intern. Med. 61, 315 (1964).PubMedGoogle Scholar
  344. Penick, P. D., Roberts, H. R., Dejanov, I. I.: Covert intravascular clotting. Fed. Proc. 24, 285 (1965).Google Scholar
  345. Pfueller, S., Somer, J. B., Castaldi, P. A.: Haemophilia due to an abnormal factor IX. Coagulation 2, 213 (1969).Google Scholar
  346. Pisano, J. J., Finlayson, J. S., Peyton, M. P.: Cross-link in fibrin polymerized by factor XIII: ε-(γ-glutamyl)lysine. Science 160, 892 (1968).PubMedGoogle Scholar
  347. Pitlick, F.: The significance of factor IX inhibition by heparin in intrinsic blood coagulation. Thesis, University of Washington (1968).Google Scholar
  348. Pool, J. G.: Antihemophilic globulin (AHG, factor VIII) activity in spleen. Fed. Proc. 25, 317 (1966).Google Scholar
  349. Pool, J. G., Hershgold, E. J., Pappenhagen, A. R.: High-potency actihaemophilic factor concentrate prepared from cryoglobulin precipitate. Nature (Lond.) 203, 312 (1964).PubMedGoogle Scholar
  350. Poole, J. C. F., Robinson, D. S.: Further observations on the effects of ethanolamine phosphatide on plasma coagulation. Quart. J. exp. Physiol. 41, 295 (1956).PubMedGoogle Scholar
  351. Prentice, C. R. M., Ratnoof, O. D., Breckenridge, R. T.: Experiments on the natur of the prothrombin-converting principle: alteration of proaccelerin by thrombin. Brit. J. Haemat. 13, 898 (1967).PubMedGoogle Scholar
  352. Prydz, H.: Studies on proconvertin (factor VII). II. Purification. Scand. J. clin. Lab. Invest. 16, 101 (1964).PubMedGoogle Scholar
  353. Prydz, H.: Some characteristics of purified factor VII preparations. Scand. J. clin. Lab. Invest. 17, Suppl. 84, 78 (1965).PubMedGoogle Scholar
  354. Prydz, H., Gladhaug, Å.: Factor X. Immunological studies. Thrombos. Diathes. haemorrh. (Stuttg.) 25, 157 (1971).Google Scholar
  355. Quick, A. J.: Calcium in the coagulation of the blood. Amer. J. Physiol. 131, 455 (1940).Google Scholar
  356. Quick, A. J.: Hemorrhagic diseases and the physiology of hemostasis. Springfield, Illinois: Charles C. Thomas 1942.Google Scholar
  357. Rapaport, S. I.: Possible relationships between clotting factors in vitro and intravascular clotting. Angiology 10, 391 (1959).PubMedGoogle Scholar
  358. Rapaport, S. I., Aas, K., Owren, P. A.: Effect of glass upon activity of various plasma clotting factors. J. clin. Invest. 34, 9 (1955).PubMedGoogle Scholar
  359. Rapaport, S. I., Ames, S. B., Mikkelsen, S.: The levels of antihemophilic globulin and proaccelerin in fresh and bank blood. Amer. J. clin. Path. 31, 297 (1955).Google Scholar
  360. Rapaport, S. I., Hjort, P. F., Patch, M. J.: Further evidence that thrombin-activation of factor VIII is an essential step in intrinsic clotting. Scand. J. clin. Lab. Invest. 17, Suppl. 84 (1965).Google Scholar
  361. Rapaport, S. I., Proctor, R. R., Patch, M. J., Yettra, M.: The mode of inheritance of PTA deficiency: evidence for the existence of major PTA deficiency and minor PTA deficiency. Blood 18, 149 (1961).PubMedGoogle Scholar
  362. Rapaport, S. I., Schiffman, I., Patch, M. J., Ames, S. B.: The importance of activation of antihemophilic globulin and proaccelerin by traces of thrombin in the generation of intrinsic prothrombinase activity. Blood 21, 221 (1963).PubMedGoogle Scholar
  363. Rapport, M. M.: Activation of phospholipid thromboplastin by lecithin. Nature (Lond.) 178, 591 (1956).PubMedGoogle Scholar
  364. Ratnoff, O. D.: The biology and pathology of the initial stages of blood coagulation. In: Progress in hematology, eds. Moore and Brown, vol. 5, p. 204. New York: Grune & Stratton 1966.Google Scholar
  365. Ratnoff, O. D., Busse, R. J., Sheon, R. P.: The demise of John Hageman. New Engl. J. Med. 279, 760 (1968).Google Scholar
  366. Ratnoff, O. D., Colopy, J. E.: A familial haemorrhagic trait associated with a deficiency of a clot promoting fraction of plasma. J. clin. Invest. 34, 602 (1955).PubMedGoogle Scholar
  367. Ratnoff, O. D., Crum, J. D.: Activation of Hageman factor by solutions of ellagic acid. J. Lab. clin. Med. 63, 359 (1964).PubMedGoogle Scholar
  368. Ratnoff, O. D., Davie, E. W.: Activation of Christmas factor (factor IX) by activated plasma thromboplastin antecedent (activated factor IX). Biochemistry 1, 677 (1962).Google Scholar
  369. Ratnoff, O. D., Davie, E. W., Mallett, D. L.: Studies on the action of Hageman factor: evidence that activated Hageman factor in turn activates plasma thromboplastin antededent. J. clin. Invest. 40, 803 (1961).PubMedGoogle Scholar
  370. Ratnoff, O. D., Miles, A. A.: The induction of permeability-increasing activity in human plasma by activated Hageman factor. Brit. J. exp. Path. 45, 328 (1964).PubMedGoogle Scholar
  371. Ratnoff, O. D., Rosenblum, J. M.: Role of Hageman factor in the initiation of clotting by glass. Amer. J. Med. 25, 160 (1958).PubMedGoogle Scholar
  372. Robbins, K. C.: A study on the conversion of fibrinogen to fibrin. Amer. J. Physiol. 142, 581 (1944).Google Scholar
  373. Roberts, H. R., Grizzle, J. E., McLester, W. D., Penick, G. D.: Genetic variants of hemophilia B: Detection by means of a specific PTC inhibitor. J. clin. Invest. 47, 360 (1968).PubMedGoogle Scholar
  374. Robinson, A. J., Aggeler, P. M., McNicol, Sp., Douglas, A. S.: An atypical genetical haemorrhagic disease with increased concentration of a natural inhibitor of prothrombin consumption. Brit. J. Haemat. 13, 150 (1967).Google Scholar
  375. Rodriguez-Erdmann, F.: Studies on the pathogenesis of the generalized Shwartzman reaction. III. Trigger mechanism for the activation of the prothrombin molecule. Thrombos. Diathes. haemorrh. (Stuttg.) 12, 471 (1964).Google Scholar
  376. Roka, L., ed.: Generalisierte intravaskuläre Gerinnung. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 50, 272 (1971).Google Scholar
  377. Rosenthal, R. L., Dreskin, O. H., Rosenthal, N.: New hemophilia-like disease caused by deficiency of a third plasma thromboplastin factor. Proc. Soc. exp. Biol. (N.Y.) 82, 171 (1953).PubMedGoogle Scholar
  378. Rosenthal, R. L., Dreskin, O. H., Rosenthal, N.: Plasma thromboplastin antecedent (P.T.A.) deficiency: Clinical, coagulation, therapeutic and hereditary aspects of a new hemophilia-like disease. Blood 10, 120 (1955).PubMedGoogle Scholar
  379. Rozenberg, F. D., Waugh, D. F.: Multiple bovine thrombin components. J. biol. Chem. 245, 5049 (1970).Google Scholar
  380. Schiffman, S., Rapaport, S. E., Patch, M. J.: Starch block electrophoresis of clotting factors. Clin. Res. 12, 110 (1964).Google Scholar
  381. Schiffman, S., Rapaport, S. I., Chong, M. M. Y.: The mandatory role of lipid in the interaction of factors 8 and 9. Proc. Soc. exp. Biol. (N.Y.) 123, 736 (1966).PubMedGoogle Scholar
  382. Schimpf, K.: In: Uterine Hämostase. Herz und Blutgerinnung. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 44, 21 (1971).Google Scholar
  383. Schmidt, A.: Über den Faserstoff und die Ursachen seiner Gerinnung. Arch. Anat. Physiol. Lpz., p. 545 (1861).Google Scholar
  384. Schmidt, A.: Neue Untersuchung über die Faserstoffgerinnung. Pflügers Arch. ges. Physiol. 6, 413 (1872).Google Scholar
  385. Schmidt, A.: Quoted by Morawitz, 1905. Zur Blutlehre, Leipzig 1892.Google Scholar
  386. Schneider, Ch. L.: Disseminated intravascular coagulation: Thrombosis versus fibrination, in clinical disease states. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 36, 1 (1969).Google Scholar
  387. Schoenmakers, J. G. G., Kurstjens, R. M., Haanen, C., Zilliken, F.: Purification of activated bovine Hageman factor. Thrombos. Diathes. haemorrh. (Stuttg.) 9, 546 (1963).Google Scholar
  388. Schoenmakers, J. G. G., Matze R., Haanen, C., Zilliken, F.: Hageman factor a novel sialoglycoprotein with esterase activity. Biochim. biophys. Acta (Amst.) 101, 166 (1965).PubMedGoogle Scholar
  389. Schwartz, M. L., Salvatore, V. P., Hill, R. L., McKee, P. A.: The subunit structures of human plasma and platelet factor XIII (Fibrin-stabilizing factor). J. biol. Chem. 246, 5851 (1971).PubMedGoogle Scholar
  390. Schwick, G., Schultze, H. E.: Immunochemische Untersuchungen mit Prothrombin und Thrombin. Clin. chim. Acta 4, 26 (1959).PubMedGoogle Scholar
  391. Seaman, A. J., Owren, P. A.: An asolectin adsorbed substrate for proaccelerin assay. J. clin. Invest. 35, 145 (1956).PubMedGoogle Scholar
  392. Seegers, W. H.: The purification of prothrombin and thrombin. Chemical properties of the purified preparations. J. biol. Chem. 136, 103 (1940).Google Scholar
  393. Seegers, W. H.: The purification of prothrombin. Record Chem. Progr. 13, 143 (1952).Google Scholar
  394. Seegers, W. H.: Prothrombin, p. 728. Cambridge, Mass.: Harvard University Press 1962.Google Scholar
  395. Seegers, W. H.: In: Blood coagulation hemorrhage and thrombosis (L. M. Tocantis and C. A. Kazal, eds.), p. 174. New York: Grune & Stratton 1964.Google Scholar
  396. Seegers, W. H.: Prothrombin in enzymology, thrombosis and hemophilia, p. 181. Springfield, Ill.: Thomas 1967.Google Scholar
  397. Seegers, W. H., Cole, E. R., Aoki, N., Harmison, C. R.: Separation of autoprothrombin III from bovine prothrombin preparations. Canad. J. Biochem. 42, 229 (1964b).PubMedGoogle Scholar
  398. Seegers, W. H., Cole, E. R., Harmison, C. R., Marciniak, E.: Purification and some properties of autoprothrombin C. Canad. J. Biochem. 41, 1047 (1963).PubMedGoogle Scholar
  399. Seegers, W. H., Cole, E. R., Harmison, C. R., Monkhouse, F. C.: Neutralization of autoprothrombin C activity with antithrombin. Canad. J. Biochem. 42, 359 (1964a).PubMedGoogle Scholar
  400. Seegers, W. H., Cole, E. R., Marciniak, E.: Partial activation of purified prothrombin: Derivation of autoprothrombin I with use of autoprothrombin C. Thrombos. Diathes. haemorrh. (Stuttg.) 7, 239 (1962).Google Scholar
  401. Seegers, W. H., Heene, D., Marciniak, E.: Activation of purified prothrombin in ammonium sulphate solutions: Purification of autoprothrombin C. Thrombos. Diathes. haemorrh. (Stuttg.) 15, 1 (1966).Google Scholar
  402. Seegers, W. H., Heene, D., Marciniak, E., Ivanovic, N., Caldwell, M. J.: Sensitivity of thrombin and autoprothrombin C to selected enzyme inhibitors. Life Sci. 4, 425 (1965b).PubMedGoogle Scholar
  403. Seegers, W. H., Landaburu, R. H., Fenichel, R. L.: Isolation of platelet/co-factor I from plasma and some properties of the preparation. Amer. J. Physiol. 190, 1 (1957).PubMedGoogle Scholar
  404. Seegers, W. H., Marciniak, E.: Some activation characteristics of the prothrombin subunit of prothrombin. Life Sci. 4, 1721 (1965).PubMedGoogle Scholar
  405. Seegers, W. H., Marciniak, E., Heene, D.: Enzyme basis of prothrombin activation (blood clotting) with an analysis of hemophilia B. Tex. Rep. Biol. Med. 23, 675 (1965a).PubMedGoogle Scholar
  406. Seegers, W. H., Marciniak, E., Kipjer, R. K., Yasunaga, K.: Isolation and some properties of prethrombin and autoprothrombin III. Arch. Biochem. Biophys. 121, 372 (1967).PubMedGoogle Scholar
  407. Seegers, W. H., Murano, G., McCoy, L., Marciniak, E.: The coagulation of blood: preliminary survey of thrombin and autoprothrombin zymogen structure. Life Sci. 8, 925 (1969).PubMedGoogle Scholar
  408. Seegers, W. H., Nieft, M. L., Loomis, E. C.: Note on the adsorption of thrombin on fibrin. Science 101, 520 (1945).PubMedGoogle Scholar
  409. Shapiro, S. S., Chodosh, B. T., Aronson, D. L.: Congenital factor X dysproteinemia: a structural disorder of coagulation factor X. J. clin. Invest. (abs.) 49, 87a (1970).Google Scholar
  410. Shapiro, S. S., Martinez, S. J., Holburn, R. H.: Congenital dysprothrombinemia: an inherited structural disorder of human prothrombin. J. clin. Invest. 48, 2251 (1969).PubMedGoogle Scholar
  411. Shapiro, S. S., Waugh, D. F.: The purification of human prothrombin. Thrombos. Diathes. haemorrh. (Stuttg.) 16, 469 (1966).Google Scholar
  412. Sharp, A. A.: Viscous metamorphosis of blood platelets: a study of the relationship to coagulation factors and fibrin formation. Brit. J. Haemat. 4, 28 (1958).PubMedGoogle Scholar
  413. Shaw, S., Pegrum, G. D., Farthing, C. P., Wolff, S.: Assessment of factor VII and factor X. Thrombos. Diathes. haemorrh. (Stuttg.) 15, 294 (1966).Google Scholar
  414. Sherman, L. A., Fletcher, A. P., Sherry, S.: In vivo transformation between fibrinogen of varying ethanol solubilities. Fed. Proc. 27, 693 (1968).Google Scholar
  415. Sherry, S., Alkjaersig, N. K., Fletcher, A. P.: Observations on the spontaneous arginine and lysine esterase activity of human plasma and their relation to Hageman factor. Thrombos. Diathes, haemorrh. (Stuttg.), Suppl. 20, 243 (1966).Google Scholar
  416. Shigeharu, N., Takahashi, H., Koida, M., Suzuki, T.: Partial purification of bovine plasma kallikreinogen, its activation by the Hageman factor. Biochem. biophys. Res. Commun. 32, 644 (1968).Google Scholar
  417. Shulman, S.: The size and shape of bovine fibrinogen. Studies on sedimentation, diffusion and viscosity. J. Amer. chem. Soc. 75, 5846 (1953).Google Scholar
  418. Shulman, S., Landaburu, R. H., Seegers, W. H.: Biophysical studies on platelet cofactor I preparations. Thrombos. Diathes. haemorrh. (Stuttg.) 4, 336 (1960).Google Scholar
  419. Shulman, I., Smith, C. H., Erlandson, M., Fort, E., Lee, R. E.: A familial hemorrhagic disease in males and females characterized by combined antihemophilic globulin deficiency and vascular abnormality. Pediatrics 18, 347 (1956).Google Scholar
  420. Simonetti, C., Casillas, G., Pavlovsky, A.: Purification du facteur VIII antihémophilique (FAH). Hémostase 1, 57 (1961).PubMedGoogle Scholar
  421. Silver, M. J., Turner, D. L., Rodalewicz, I., Giordano, N., Holburn, R., Herb, S. F., Luckly, F. E.: Evaluation of activity of phospholipids in blood coagulation in vitro. Thrombos. Diathes. haemorrh. (Stuttg.) 10, 164 (1963).Google Scholar
  422. Soulier, J.-P., Menache, D., Steinbuch, M., Blatrix, C. H., Josso, F.: Preparation and clinical use of PPSB (factors II, VII, X and IX concentrate). Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 35, 69 (1969).Google Scholar
  423. Soulier, J.-P., Prou-Wartelle, O.: Preparation of a serum fraction rich in convertin (VII), Stuart factor (X) and antihemophilic B factor (IX). Fraction B.S.C. Experimental study in the rabbit. Nouv. Rev. franç. Hémat. 2, 27 (1962).PubMedGoogle Scholar
  424. Soulier, J.-P., Prou-Wartelle, O.: New data on Hageman factor and plasma thromboplastin antedecent. The role of contact in the initial phase of blood coagulation. Brit. J. Haemat. 6, 88 (1960).Google Scholar
  425. Soulier, J.-P., Prou-Wartelle, O., Menache, D.: Caractères différentiels des facterus Hageman et P.T.A. role du contact dans la phase initiale de la coagulation. Rev. franç. Étud. clin. biol. 3, 263 (1958).PubMedGoogle Scholar
  426. Soulier, J.-P., Prou-Wartelle, O., Menache, D.: Hageman trait and PTA deficiency. The role of contact of blood with glass. Brit. J. Haemat. 5, 121 (1959).PubMedGoogle Scholar
  427. Speer, R. J., Ridgway, H., Hill, M. J.: Activated human Hageman factor. Thrombos. Diathes. haemorrh. (Stuttg.) 14, 1 (1965).Google Scholar
  428. Spittel, J. A., Pascuzzi, C. A., Thompson, J. H., Jr., Owen, C. A., Jr.: Acceleration of early stages of coagulation in certain patients with occlusive arterial or venous diseases: use of a modified thromboplastin generation test to evaluate clot. Proc. Mayo Clin. 35, 37 (1960).Google Scholar
  429. Stites, D. P., Hershgold, E. J., Perlman, J. D., Fudenberg, M. M.: Factor VIII detection by hemagglutination inhibition. Hemophilia A and von Willebrand’s disease. Science 171, 196 (1971).PubMedGoogle Scholar
  430. Stormorken, H.: Species differences of clotting factors in ox, dog, horse and man. Proaccelerin and accelerin. Acta physiol. scand. 39, 121 (1957).PubMedGoogle Scholar
  431. Stormorken, H.: The defect in von Willebrand’s disease. In: Physiology of hemostasis and thrombosis (Johnson, S. A., Seegers, W. H., eds.), p. 179. Springfield, Ill. C. C. Thomas 1967.Google Scholar
  432. Straub, W., Duckert, F.: The formation of the extrinsic prothrombin activator. Thrombos. Diathes. haemorrh. (Stuttg.) 5, 402 (1961).Google Scholar
  433. Stryer, L., Cohen, C., Langridge, R.: Axial period of fibrinogen and fibrin. Nature (Lond.) 197, 793 (1963).PubMedGoogle Scholar
  434. Surgenor, D. M., Wilson, N. A., Henry, A. S.: Factor V from human plasma. Thrombos. Diathes. haemorrh. (Stuttg.) 5, 1 (1961).Google Scholar
  435. Telfer, T. P., Denson, K. W., Wright, D. R.: A “new” coagulation defect. Brit. J. Haemat. 2, 308 (1956).PubMedGoogle Scholar
  436. Thompson, A. R., Davie, E. W.: Affinity chromatography of thrombin. Biochim. biophys. Acta (Amst.) 250, 210 (1971).PubMedGoogle Scholar
  437. Tishkoff, G. H., Pechet, L., Alexander, B.: Some biochemical and electrophoretic studies on purified prothrombin, factor VII and factor X. Blood 15, 778 (1960).PubMedGoogle Scholar
  438. Tishkoff, G. H., Williams, L. C., Brown, D. M.: Preparation of highly purified prothrombin complex. I. Crystallization, biological activity, and molecular properties. J. biol. Chem. 243, 4151 (1968).PubMedGoogle Scholar
  439. Triantaphyllopoulos, D. C., Chen, E., Triantaphyllopoulos, E.: Nature of inhibition of prothrombin/consumption by lysed fibrinogen. Brit. J. Haemat. 16, 589 (1969).PubMedGoogle Scholar
  440. Troup, S. B., Reed, C. F., Marinetti, G. V., Swischer, S. N.: Thromboplastin factors in platelets and red blood cells: observations on their chemical nature and function in in vitro coagulation. J. clin. Invest. 39, 342 (1960).PubMedGoogle Scholar
  441. Turner, D. L., Silver, M. J.: Total synthesis of unsaturated phosphatidyl-serine and its activity in clotting systems. Nature (Lond.) 200, 370 (1963).PubMedGoogle Scholar
  442. Veltkamp, J. J., Drion, E. F., Loeliger, E. A.: Detection of the carrier state in hereditary coagulation disorders. Thrombos. Diathes. haemorrh. (Stuttg.) 19, 279, 403 (1968).Google Scholar
  443. Veltkamp, J. J., Meilof, J., Rammelts, H. G., van der Vlerk, D., Loeliger, E. A.: Another genetic variant of haemophilia B. Haemophilia B Leyden. Scand. J. Haemat. 7, 82 (1970).PubMedGoogle Scholar
  444. Veltkamp, J. J., Muis, H., Muller, A. D., Hemker, H. C., Loeliger, E. A.: Additional evidence for the existence of a precursor molecule of the prothrombin complex in oral anticoagulation. Thrombos. Diathes. haemorrh. (Stuttg.) 25, 312 (1971).Google Scholar
  445. Verstraete, M., Vermylen, J., Donati, M. B., eds.: Fibrinogen degradation products. Scand. J. Haemat., Suppl. 13, 392 (1971).Google Scholar
  446. Vinazzer, H., Reinhardt, F.: On the nature of anti-thrombin V. Thrombos. Diathes. haemorrh. (Stuttg.) 20, 234 (1968).Google Scholar
  447. Vroman, L.: To be added in proof. Thesis, University of Utrecht, 1958.Google Scholar
  448. Vroman, L.: Behavior of coagulation factors at interfaces. In: Biophysical mechanism in vascular homeostasis and intravascular thrombosis (P. N. Sawyer, ed.), p. 81. New York: Appleton 1965.Google Scholar
  449. Vroman, L.: Surface activity in blood coagulation. In: Blood clotting enzymology (W. H. Seegers ed.), p. 279. New York: Academic Press 1967.Google Scholar
  450. Vroman, L.: Biological aspects of surface activation. Thrombos. Diathes. haemorrh. (Stuttg.), Suppl. 25, 89 (1968).Google Scholar
  451. Waaler, B. A.: Contact activation in the intrinsic blood clotting system. Studies on a plasma product formed on contact with glass and similar surfaces. Thesis. Oslo University Press, 1959, p. 133. Scand. J. clin. Lab. Invest. 11 (Suppl. 37) (1959).Google Scholar
  452. Walls, W. D., Losowsky, M. S.: Congenital deficiency of fibrin stabilizing factor. Coagulation 1, III (1968).Google Scholar
  453. Walsh, P. N.: The role of platelets in the contact phase of blood coagulation. Brit. J. Haemat. 22, 237 (1972).PubMedGoogle Scholar
  454. Ware, A. G., Murphy, R. C., Seegers, W. H.: The function of Ac-globulin in clotting. Science 106, 618 (1947).PubMedGoogle Scholar
  455. Ware, A. G., Seegers, W. H.: Plasma accelerator globulin: partial purification, quantitative determination and properties. J. biol. Chem. 72, 699 (1948).Google Scholar
  456. Wessler, S., Reimer, S. M., Bloede, M., Nickles, M., Szlat, B. J.: The role of human coagulation factors in serum-induced thrombosis. J. clin. Invest. 39, 262 (1960).PubMedGoogle Scholar
  457. Williams, W. J., Esnouf, M. P.: The fractionation of Russell’s viper (Vipera russellii) venom with special reference to the coagulant protein. Biochem. J. 84, 52 (1962).PubMedGoogle Scholar
  458. Williams, W. J., Norris, D. G.: Purification of a bovine plasma-protein factor (VII) which is required for the activity of lung microsomes in blood coagulation. J. biol. Chem. 241, 1847 (1966).PubMedGoogle Scholar
  459. Wilner, G. D., Nossel, H. L., de Roy, C. C.: Activation of Hageman factor by collagen. J. clin. Invest. 47, 2608 (1968).PubMedGoogle Scholar
  460. Wöhlisch, E.: Die Physiologie und Pathologie der Blutgerinnung. Ergebn. Physiol. 28, 443 (1929).Google Scholar
  461. Wright, A. E.: On a method of determining the condition of blood coagulability for clinical and experimental purposes, and on the effect of the administration of calcium salts in haemophilia and actual or threatened haemorrhage. Brit. med. J. 1893 II, 223.Google Scholar
  462. Yin, E. T., Wessler, S.: Heparin-accelerated inhibition of activated factor X by its natural plasma inhibitor. Biochim. biophys. Acta (Amst.) 201, 387 (1970).PubMedGoogle Scholar
  463. Zimmerman, T. S., Arroyave, C. M., Müller-Eberhard, H. J.: A blood coagulation abnormality in rabbits deficient in the sixth component of complement (C 6) and its correction by purified C 6. J. exp. Med. 134, 1591 (1971).PubMedGoogle Scholar
  464. Zimmerman, T. S., Ratnoff, O. D., Powell, A. E.: Immunologic differentiation of classic hemophilia (Factor VIII deficiency) and von Willebrand’s disease. J. clin. Invest. 50, 244 (1971).PubMedGoogle Scholar

Copyright information

© Springer-Verlag 1973

Authors and Affiliations

  • P. A. Owren
  • H. Stormorken
    • 1
  1. 1.The University Institute for Thrombosis Research, RikshospitaletOsloNorway

Personalised recommendations