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The Coagulation System

  • Derek Ogston

Abstract

The classical intrinsic coagulation pathway is initiated by the activation of factor XII. This unique protein is also known as Hageman factor from che name of the patient in whom its deficiency was first recognised (Ratnoff and Colopy, 1955; Ratnoff and Rosenblum, 1958). Factor XII is also involved in one pathway leading to the generation of an activator of plasminogen (Niewiarowski and Prou-Wartelle, 1959), discussed in Chapter 4, and in the formation of kinins (Margolis, 1958).

Keywords

Factor Versus Coagulation System Fibrinogen Degradation Product Plasma Kallikrein Fibrinogen Synthesis 
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.

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References

  1. Albildgaard, U. (1967) ‘Purification of two progressive antithrombins of human plasma’, Scandinavian Journal of Clinical and Laboratory Investigation, 19, 190–5CrossRefGoogle Scholar
  2. Abildgaard, U. (1968) ‘Highly purified antithrombin III with heparin cofactor activity prepared by disc electrophoresis’, Scandinavian Journal of Clinical and Laboratory Investigation, 21, 89–91CrossRefGoogle Scholar
  3. Abildgaard, U. (1969) ‘Binding of thrombin to antithrombin HI’, Scandinavian Journal of Clinical and Laboratory Investigation, 24, 23–7CrossRefGoogle Scholar
  4. Aguercif, M., Giacometti, N., Nigg, O.M., Lacourt, G. and Bouvier, C.A. (1973) ‘Existetil un fibrinogene foetal? Explanation statistique de la fibrinoformation dans une population de nouveaunes prematures, matures et post-matures’, Pediatric 28, 381–99Google Scholar
  5. Alkjaersig, N., Fletcher, A.P. and Sherry, S. (1962) ‘Pathogenesis of the coagulation defect developing during pathological plasma proteolytic (“fibrinolytic”) states. II. The significance, mechanism and consequences of defective fibrin polymerisation’, Journal of Clinical Investigation, 41, 917–34CrossRefGoogle Scholar
  6. Alving, B.M., Bell, W.R. and Evatt, B.L. (1977a) ‘Fibrinogen synthesis in rabbits: effects of altered levels of circulating fibrinogen’, American Journal of Physiology, 232, 478–484Google Scholar
  7. Alving, B.M., Evatt, B.L. and Bell, W.R. (1977b) ‘Stimulation of fibrinogen synthesis in rabbits with ancrod-induced afibrinogenemia’, American Journal of Physiology, 233, 562–567Google Scholar
  8. Andersson, L.-O., Barrowcliffe, T.W., Holmer, E., Johnson, E.A. and Sims, G.E.C. (1976) ‘Anticoagulant properties of heparin fractionated by affinity chromatography on matrix-bound antithrombin-III and by gel filtration’, Thrombosis Research, 9, 575–83CrossRefGoogle Scholar
  9. Andersson, L.-O., Engman, L. and Henningsson, E. (1977) ‘Crossed Immunoelectrophoresis as applied to studies on complex formation. The binding of heparin to antithrombin III and the antithrombin-thrombin complex’, Journal of Immunological Methods, 14, 271–81CrossRefGoogle Scholar
  10. Andersson, L.-O., Barrowcliffe, T.W., Holmer, E., Johnson, E.A. and Söderström, G. (1979) ‘Molecular weight dependency of the heparin potentiated inhibition of thrombin and activated factor X. Effect of heparin neutralization in plasma’, Thrombosis Research, 75, 531–41CrossRefGoogle Scholar
  11. Aronson, D.L., Stevan, L., Ball, A.P., Franza, B.R. and Finlayson, J.S. (1977) ‘Generation of the combined prothrombin activation peptide (F 1.2) during the clotting of blood and plasma’, Journal of Clinical Investigation, 60, 1410–8CrossRefGoogle Scholar
  12. Aronson, D.L., Ball, A.P., Franza, R.B., Hugh, T.E. and Fenton, J.W. II (1980) ‘Human prothrombin fragments in F 1 (aß) and F 2: preparation and characterization of structural and biological properties’, Thrombosis Research, 20, 239–53CrossRefGoogle Scholar
  13. Atencio, A.C. and Lorand, L. (1970) ‘Effect of ACTH on biosynthesis of fibrinogen in the rabbit’, American Journal of Physiology, 219, 1161–5Google Scholar
  14. Atencio, A.C., Joiner, K. and Reeve, E.B. (1969a) ‘Experimental and control systems studies of plasma fibrinogen regulation in rabbits’, American Journal of Physiology, 216, 764–72Google Scholar
  15. Atencio, A.C., Chao, P.-Y., Chen, A. and Reeve, E.B. (1969b) ‘The fibrinogen response to corticotropin preparations in rabbits’, American Journal of Physiology, 216, 773–80Google Scholar
  16. Awbrey, B.J., Hoak, T.C. and Owen, W.G. (1979) ‘Binding of human thrombin to cultured human endothelial cells’, Journal of Biological Chemistry, 254, 4092–5Google Scholar
  17. Ayotte, L., Lorimeau, J.C. and Perlin, A.S. (1981) ‘Influence of variations in the chemical structure of heparin on its anticoagulant and anti-factor Xa activities’, Thrombosis Research, 22, 97–102CrossRefGoogle Scholar
  18. Bach, R., Nemerson, Y. and Königsberg, W. (1981) ‘Purification and characterization of bovine tissue factor’, Journal of Biological Chemistry, 256, 8324–31Google Scholar
  19. Bachmann, L., Schmitt-Fumian, W., Hammel, R. and Lederer, K. (1975) ‘Size and shape of fibrinogen. I. Electron microscopy of the hydrated molecule’, Die Makromokulare Chemie, 176, 2603–18CrossRefGoogle Scholar
  20. Bagdasarian, A., Lahiri, B., Talamo, R.G., Wong, P. and Colman, R.W. (1974) ‘Immunochemical studies of plasma kallikrein’, Journal of Clinical Investigation, 54, 1444–54CrossRefGoogle Scholar
  21. Bajaj, S.P., Rapaport, S.I. and Brown, S.F. (1981) ‘Isolation and characterization of human factor VII. Activation of factor VII by factor Xa’, Journal of Biological Chemistry, 256, 253–9Google Scholar
  22. Barnhart, M.I. and Anderson, G.F. (1962) ‘Intracellular localization of fibrinogen’, Proceedings of the Society for Experimental Biology and Medicine, 110, 734–7Google Scholar
  23. Barnhart, M.I., Cress, D.C., Noonan, S.M. and Walsh, R.T. (1970) ‘Influence of fibrinolytic products on hepatic release and synthesis of fibrinogen’, Thrombosis et Diathesis Haemorrhagica, Suppl. 39, 143–59Google Scholar
  24. Barrowcliffe, T.W. and Eggleton, C.A. (1981) ‘The anti-Xa activity of lipoproteins’, Thrombosis and Haemostasis, 46, 351Google Scholar
  25. Bartlett, S., Latson, P. and Hanahan, D.J. (1980) ‘High molecular weight factor V of bovine and human plasma’, Biochemistry, 19, 273–7CrossRefGoogle Scholar
  26. Bergqvist, D. and Nilsson, I.M. (1979) ‘A family with oc2-macroglobulin deficiency’, Thrombosis and Haemostasis, 42, 249Google Scholar
  27. Bettelheim, F.R. and Bailey, K. (1952) ‘The products of the action of thrombin on fibrinogen’, Biochimica et Biophysica Acta, 9, 578–9CrossRefGoogle Scholar
  28. Biggs, R., Denson, K.W.E., Akman, N., Barrett, R. and Hadden, M. (1970) ‘Antithrombin III, anti-factor Xa and heparin’, British Journal of Haematology, 79, 283–305CrossRefGoogle Scholar
  29. Bilezikian, S.B., Nossel, H.L., Butler, V.P. and Canfield, R.E. (1975) ‘Radioimmunoassay of human fibrinopeptide B and kinetics of fibrinopeptide cleavage by different enzymes’, Journal of Clinical Investigation, 56, 438–45CrossRefGoogle Scholar
  30. Björk, I., Danielsson, Ä., Fish, W.W., Larsson, K., Lieden, K. and Nordenman, B. (1979) ‘The interaction between heparin and antithrombin’, in D. Collen, B. Wiman and M. Verstraete (eds.) The Physiological Inhibitors of Blood Coagulation and Fibrinolysis, Elsevier/North Holland, Amsterdam, pp. 67–84Google Scholar
  31. Björk, L, Jackson, CM., Jornvall, H., Lavine, K.K., Nordling, K. and Salsgiver, W.J. (1981) ‘The active site of antithrombin. Release of the same proteolytically cleaved form of the inhibitor from complexes with factor IXa, factor Xa and thrombin’, Thrombosis and Haemostasis, 46, 286Google Scholar
  32. Bjorklid, E. and Storm, E. (1977) ‘Purification and some properties of the protein component of tissue thromboplastin from human brain’, Biochemical Journal, 165, 89–96Google Scholar
  33. Blombäck, B. and Vestermark, A. (1958) ‘Isolation of fibrinopeptides by chromatography’, Arkiv for Kemi, 12, 173–83Google Scholar
  34. Blombäck, B., Blombäck, M. Henschen, A., Hessel, B., Iwanaga, S. and Woods, K.R. ‘N-terminal disulphide knot of human fibrinogen’, Nature, 218, 130–4Google Scholar
  35. Blombäck, B., Hessel, B. and Hogg, D. (1976) ‘Disulphide bridges in NH2-terminal part of human fibrinogen’, Thrombosis Research, 8, 639–58CrossRefGoogle Scholar
  36. Blombäck, B., Hessel, B., Hogg, D. and Therkildsen, L. (1978) ‘A two-step fibrinogen-fibrin transition in blood coagulation’, Nature, 275, 501–5CrossRefGoogle Scholar
  37. Bocci, V. and Pacini, A. (1973) ‘Factors regulating plasma protein synthesis. II. Influence of fibrinogenolytic products on plasma fibrinogen concentration’, Thrombosis et Diathesis Haemorrhagica, 29, 63–75Google Scholar
  38. Bocci, M., Conti, T., Muscellota, M., Pacini, A. and Pessina, G.P. (1974) ‘Factors regulating plasma protein synthesis. IV. Influence of fragments D and E on plasma fibrinogen concentrations’, Thrombosis et Diathesis Haemorrhagica, 31, 395–402Google Scholar
  39. Bocci, M., Muscettoia, M., Pacini, A. and Pessina, G.P. (1976) ‘The effect of leucocyte pyrogen on rabbit fibrinogen. A third view’, Thrombosis Research, 9, 505–12CrossRefGoogle Scholar
  40. Bohn, H. (1972) ‘Comparative studies on the fibrin-stabilizing factors from human plasma, platelets and placentas’, Annals of the New York Academy of Sciences, 202, 256–72CrossRefGoogle Scholar
  41. Bohn, H. (1974) ‘Immunologische Untersuchungen über Faktor XIII und das PSF-bindende Globulin’, Blut, 28, 81–90CrossRefGoogle Scholar
  42. Bouma, B.N. and Griffin, J.H. (1977) ‘Human blood coagulation factor XI. Purification, properties, and mechanism of activation by activated factor XII’, Journal of Biological Chemistry, 252, 6432–6437Google Scholar
  43. Bouma, B.N., Miles, L.A., Beretta, G. and Griffin, J.H. (1980) ‘Human plasma prekallikrein. Studies of its activation by activated factor XII and of its inactivation by diisopropyl phosphofluoridate’, Biochemistry, 19, 1151–60CrossRefGoogle Scholar
  44. Bouma, H., Takagi, T. and Doolittle, R.F. (1978) ‘The arrangement of disulphide bonds in fragment D from human fibrinogen’, Thrombosis Research, 13, 557–62CrossRefGoogle Scholar
  45. Bounassisi, V. (1973) ‘Sulfated mucopolysaccharide synthesis and secretion in endothelial cell cultures’, Experimental Cell Research, 76, 363–8CrossRefGoogle Scholar
  46. Bowie, E.J.W., Woods, J.E., Fass, D.N., Zollman, P.E. and Owen, CA. (1975) ‘Liver transplantation in pigs with von Willebrand’s disease’, British Journal of Haematology, 31, 31–44CrossRefGoogle Scholar
  47. Breederveld, K., Giddngs, J.C, ten Cate, J.W. and Bloom, A.L. (1975) ‘The localisation of factor V within normal human platelets and the demonstration of a platelet-factor V antigen in congenital factor V deficiency’, British Journal of Haematology, 29,405–12CrossRefGoogle Scholar
  48. Broze, G.J. and Majerus, P.W. (1980) ‘Purification and properties of human coagulation factor VII’, Journal of Biological Chemistry, 255, 1242–1247Google Scholar
  49. Bucher, D., Nebelin, E., Thomsen, J. and Stenflo, J. (1976) ‘Identification of y-carboxyglutamic acid residues in bovine factors IX and X, and in a new vitamin K-dependent protein’, FE BS Letters, 68, 293–296CrossRefGoogle Scholar
  50. Budzynski, A. (1971) ‘Difference in conformation of fibrinogen degradation products as revealed by hydrogen exchange and spectropolarimetry’, Biochimica et Biophysica Acta, 229, 663–71Google Scholar
  51. Bundy, H.F. and Mehl, J.W. (1959) ‘Trypsin inhibitors of human serum’, Journal of Biological Chemistry, 234, 1124–8Google Scholar
  52. Burrowes, C.E., Habal, F.M. and Movat, H.Z. (1975) ‘The inhibition of human plasma kallikrein by antithrombin III’, Thrombosis Research, 7, 175–83CrossRefGoogle Scholar
  53. Butkowski, R.J., Elion, J., Downing, M.R. and Mann, K.G. (1977) ‘Primary structure of human prethrombin 2 and a-thrombin’, Journal of Biological Chemistry, 252, 4942–57Google Scholar
  54. Campbell, J., Hausler, H.E., Munroe, J.S. and Davidson, I.W.F. (1953) ‘Effect of growth hormone in dogs’, Endocrinology, 53, 134–62CrossRefGoogle Scholar
  55. Canfield, W., Nesheim, M., Kisiel, W. and Mann, K.G. (1978) ‘Proteolytic inactivation of bovine factor Va by bovine activated protein C’, Circulation, 58, 11–210Google Scholar
  56. Carlson, T.H., Fradl, D.C., Leonard, B.D., Wentland, S.H. and Reeve, E.B. (1977) ‘Fibrinogen synthesis stimulation by prostaglandin E, and some other vasodilators’, American Journal of Physiology, 233, Hl-9Google Scholar
  57. Carrell, R.W., Jeppsson, J.-O., Laureil, C.-B., Brennan, S.O., Owen, M.C., Vaughan, L. and Boswell, D.R. (1982) ‘Structure and variation of human antitrypsin’, Nature, 298, 329–34CrossRefGoogle Scholar
  58. Castillo, R., Maragall, S., Rodes, J., demente, C, Profitös, J. and Ordinas, A. (1977) ‘Increased factor VIII complex and defective ristocetin-induced platelet aggregation in liver disease’, Thrombosis Research, 11, 899–906CrossRefGoogle Scholar
  59. Chan, J.Y.C. (1976) ‘Purification of factor XII (Hageman factor) from human plasma’, Thrombosis Research, 8, 337–49CrossRefGoogle Scholar
  60. Chan, J.Y.C, Burrowes, C.E., Habal, F.M. and Movat, H.Z. (1977) ‘The inhibition of activated factor XII (Hageman factor) by antithrombin III: the effect of other plasma proteinase inhibitors’, Biochemical and Biophysical Research Communications, 74, 150–8CrossRefGoogle Scholar
  61. Chan, J.Y.C, Movat, H.Z. (1976) ‘Purification of factor XII (Hageman factor) from human plasma’, Thrombosis Research, 8, 337–49CrossRefGoogle Scholar
  62. Chan, V. and Chan, T.K. (1979) ‘Antithrombin III in fresh and cultured human endothelial cells: a natural anticoagulant from the vascular endothelium’, Thrombosis Research, 15, 209–13CrossRefGoogle Scholar
  63. Chan, V., Chan, T.K., Wong, V., Tso, S.C and Todd, D. (1979) ‘The determination of antithrombin III by radioimmunoassay and its clinical application’, British Journal of Haematology, 41, 563–72CrossRefGoogle Scholar
  64. Chargaff, E., Bendich, A. and Cohen, S.S. (1944) ‘The thromboplastic protein: structure, properties, disintegration’, Journal of Biological Chemistry, 156, 161–78Google Scholar
  65. Chen, Y., Briese, F.W. and Reeve, E.B. (1974) ‘Relation of fibrinogen secretion (synthesis) to ACTH dose’, American Journal of Physiology, 227, 927–61Google Scholar
  66. Chesney, CM., Pifer, D. and Colman, R.W. (1981) ‘Subcellular localisation and secretion of factor V from human platelets’, Proceedings of the National Academy of Sciences, 78, 5180–4CrossRefGoogle Scholar
  67. Chuang, T.F., Sargeant, R.B. and Hougie, C. (1974) ‘The effect of calcium ions on the properties of factor IX and its activated form’, British Journal of Haematology, 27, 281–7CrossRefGoogle Scholar
  68. Claeys, H. and Collen, D. (1978) ‘Purification and characterization of bovine coagulation factor XII (Hageman factor)’, European Journal of Biochemistry, 87, 69–74CrossRefGoogle Scholar
  69. Cofrancesco, E., Radaelli, F., Pogliani, E., Amici, N., Torri, G.G. and Casu, B. (1979) ‘Correlation of sulfate content and degree of carboxylation of heparin and related glycosaminoglycans with anticomplement activity. Relationships to the anticoagulant and platelet-aggregating activities’, Thrombosis Research, 14, 179–87CrossRefGoogle Scholar
  70. Cohen, I., Blankenberg, T.A., Borden, D., and Veis, A. (1979) ‘Factor XHIa-catalysed cross-linking of platelet and muscle actin. Regulation by adenosine triphosphate’, Thrombosis and Haemostasis, 42, 395Google Scholar
  71. Collen, D., Schetz, J., de Cock, F. and Holmer, E. (1977) ‘Metabolism of antithrombin III (heparin cofactor) in man: effects of venous thrombosis and of heparin administration’, European Journal of Clinical Investigation, 7, 27–35CrossRefGoogle Scholar
  72. Colman, R.W., Bagdasarian, A., Talamo, R.C, Scott, C.F., Seavey, M., Guimaräes, J.A., Pierce, J.V. and Kaplan, A.P. (1975) ‘Williams trait. Human kininogen deficiency with diminished levels of plasminogen proactivator and prekallikrein associated with abnormalities of the Hageman factor-dependent pathways’, Journal of Clinical Investigation, 56, 1650–62CrossRefGoogle Scholar
  73. Comp, P.C. and Esmon, CT. (1979) ‘Activated protein C inhibits platelet prothrombin-converting activity’, Blood, 54, 1272–81Google Scholar
  74. Comp, P.C. and Esmon, CT. (1981) ‘Generation of fibrinolytic activity by the infusion of activated protein C into dogs’, Journal of Clinical Investigation, 68, 1221–8CrossRefGoogle Scholar
  75. Comp, P.C., Jacocks, R.M., Ferrell, G.L. and Esmon, CT. (1982) ‘Activation of protein C in vivo’, Journal of Clinical Investigation, 70, 127–34CrossRefGoogle Scholar
  76. Cottrell, B.A., Strong, D.D., Watt, K.W.K, and Doolittle, R.F. (1979) ‘Amino acid sequence studies on the a chain of human fibrinogen. Exact location of cross-linking acceptor sites’, Biochemistry, 18, 5405–10CrossRefGoogle Scholar
  77. Counts, R.B., Paskell, S.L. and Elgee, S.K. (1978) ‘Disulfide bonds and the quaternary structure of factor VIII/von Willebrand factor’, Journal of Clinical Investigation, 62, 702–9CrossRefGoogle Scholar
  78. Crawford, LP. (1973) ‘Purification and properties of normal human a j-antitrypsin’, Archives of Biochemistry and Biophysics, 156, 215–22CrossRefGoogle Scholar
  79. Credo, R.B., Curtis, CG. and Lorand, L. (1978) ‘Ca2+-related regulatory function of fibrinogen’, Proceedings of the National Academy of Sciences, 75, 4234–7CrossRefGoogle Scholar
  80. Credo, R.B., Curtis, CG. and Lorand, L. (1981) ‘oc-chain domain of fibrinogen controls generation of fibrinoligase (coagulation factor XHIa). Calcium ion regulatory aspects’, Biochemistry, 20, 3770–8CrossRefGoogle Scholar
  81. Dahlbäck, B. (1980) ‘Human coagulation factor V purification and thrombin-catalyzed activation’, Journal of Clinical Investigation, 66, 583–91CrossRefGoogle Scholar
  82. Dahlbäck, B. and Stenflo, J. (1978) ‘Binding of bovine coagulation factor Xa to platelets’, Biochemistry, 17, 4938–45CrossRefGoogle Scholar
  83. Dahlbäck, B. and Stenflo, J. (1980) ‘Inhibitory effect of activated protein C on activation of prothrombin by platelet-bound factor Xa’, European Journal of Biochemistry, 107, 331–5CrossRefGoogle Scholar
  84. Dam, H. (1935) ‘The antihaemorrhagic vitamin of the chick’, Journal of Biochemistry, 29, 1273–85Google Scholar
  85. Damus, P.S., Hicks, M. and Rosenberg, R.D. (1973) ‘Anticoagulant action of heparin’, Nature, 246, 355–7CrossRefGoogle Scholar
  86. Danielsson, A. and Björk, I. (1978) ‘The binding of low-affinity and high-affinity heparin to antithrombin’, European Journal of Biochemistry, 90, 7–12CrossRefGoogle Scholar
  87. Danishefsky, I., Zweben, A. and Slomiany, B.L. (1978) ‘Human antithrombin III. Carbohydrate components and associated glycolipid’, Journal of Biological Chemistry, 253, 32–7Google Scholar
  88. Debanne, M.T., Bell, R. and Dolovich, J. (1975) ‘Uptake of proteinase- a-macroglobulin complexes by macrophages’, Biochimica et Biophysica Acta, 411, 295–304CrossRefGoogle Scholar
  89. Debanne, M.T., Bell, R. and Dolovich, J. (1976) ‘Characteristics of the macrophage uptake of proteinase-a-macroglobulin complexes’, Biochimica et Biophysica Acta, 428, 466–75CrossRefGoogle Scholar
  90. Deuel, T.F., Senior, R.M., Chang, D., Griffin, G.L., Heinrikson, R.L. and Kaiser, E.T. (1981) ‘Platelet factor 4 is chemotactic for neutrophils and monocytes’, Proceedings of the National Academy of Sciences, 78, 4584–7CrossRefGoogle Scholar
  91. van Dieijen, G., Tans, G., Rosing, J. and Hemker, H.C. (1981) ‘The role of phospholipid and factor Villa in the activation of bovine factor X’, Journal of Biological Chemistry, 256, 3433–42Google Scholar
  92. Di Scipio, R.G. and Davie, E.W. (1979) ‘Characterization of protein S, a y-carboxyglutamic acid containing protein from bovine and human plasma’, Biochemistry, 18, 899–904CrossRefGoogle Scholar
  93. Di Scipio, R.G., Hermodson, M.A., Yates, S.G. and Davie, E.W. (1977) ‘A comparison of human prothrombin, factor IX (Christmas factor), factor X (Stuart factor), and protein S’, Biochemistry, 16, 698–706CrossRefGoogle Scholar
  94. Di Scipio, R.G., Kurachi, K. and Davie, E.W. (1978) ‘Activation of human factor IX (Christmas factor)’, Journal of Clinical Investigation, 61, 1528–38CrossRefGoogle Scholar
  95. Dodds, W.J. (1969) ‘Hepatic influence on splenic synthesis and release of coagulation activities’, Science, 166, 882–3CrossRefGoogle Scholar
  96. Dodds, W.J. and Hoyer, L.W. (1974) ‘Coagulation activities in perfused organs: regulation by addition of animal plasmas’, British Journal of Haematology, 26, 497–509CrossRefGoogle Scholar
  97. Donaldson, V.H., Kleniewski, J., Saito, H. and Sayed, J.K. (1977) ‘Prekallikrein deficiency in a kindred with kininogen deficiency and Fitzgerald trait clotting defect. Evidence that high molecular weight kininogen and prekallikrein exist as a complex in normal human plasma’, Journal of Clinical Investigation, 60, 571–83CrossRefGoogle Scholar
  98. Donovan, J.W. and Mihalyi, E. (1974) ‘Conformation of fibrinogen: calorimetric evidence for a three-nodular structure’, Proceedings of the National Academy of Sciences, 71, 4125–8CrossRefGoogle Scholar
  99. Doolittle, R.F. (1981) ‘Fibrinogen and fibrin’, in A.L. Bloom and D.P. Thomas (eds.) Haemostasis and Thrombosis, Churchill Livingstone, Edinburgh, pp. 163–91Google Scholar
  100. Doolittle, R.F., Cassman, K.G., Chen, R., Sharp, J.J. and Wooding, G.L. (1972) ‘Correlation of the mode of fibrin polymerization with the pattern of cross-linking’, Annals of the New York Academy of Sciences, 202, 114–26CrossRefGoogle Scholar
  101. Doolittle, R.F., Cassman, K.G., Cottrell, B.A., Friezner, S.J., Hucko, J.T. and Takagi, T. (1977) ‘Amino acid sequence studies on the a-chain of human fibrinogen. Characterization of eleven cyanogen bromide fragments’, Biochemistry, 16, 1703–9CrossRefGoogle Scholar
  102. Doolittle, R.F., Goldbaum, D.M. and Doolittle, L.R. (1978) ‘Designation of sequences involved in the “coiled coil” interdomainal connector in fibrinogen: construction of an atomic scale model’, Journal of Molecular Biology, 120, 311–25CrossRefGoogle Scholar
  103. Doolittle, R.F., Watt, K.W.K., Cottrell, B.A., Strong, D.D. and Riley, M. (1979) ‘The amino acid sequence of the a-chain of human fibrinogen’, Nature, 280, 464–8CrossRefGoogle Scholar
  104. Doucet-de Bruine, M.H.M., Sixma, J.J., Over, J. and Beeser-Visser, N.H. (1978) ‘Heterogeneity of human factor VIII. II. Characterization of forms of factor VIII binding to platelets in the presence of ristocetin’, Journal of Laboratory and Clinical Medicine, 92, 96–107Google Scholar
  105. Dunn, J.T., Silverberg, M. and Kaplan, A.P. (1982) ‘The cleavage and formation of acvtivated human Hageman factor by autodigestion and by kallikrein’, Journal of Biological Chemistry, 257, 1779–84Google Scholar
  106. Egeberg, O. (1965) ‘Inherited antithrombin deficiency causing thrombophilia’, Thrombosis et Diathesis Haemorrhagica, 13, 516–30Google Scholar
  107. Einarsson, R. and Andersson, L.-O. (1977) ‘Binding of heparin to human antithrombin III as studied by measurements of tryptophan fluorescence’, Biochimica et Biophysica Acta, 490, 104–11Google Scholar
  108. Enfield, D.L., Ericsson, L.H., Walsh, K.A., Neurath, H. and Titani, K. (1975) ‘Bovine factor X x (Stuart factor). Primary structure of the light chain’, Proceedings of the National Academy of Sciences, 72, 16–9CrossRefGoogle Scholar
  109. Esmon, C.T. (1979) ‘The subunit structure of thrombin-activated factor V. Isolation of activated factor V, separation of subunits, and reconstitution of biological activity’, Journal of Biological Chemistry, 254, 964–73Google Scholar
  110. Esmon, C.T. and Jackson, CM. (1974) ‘The conversion of prothrombin to thrombin IV. The function of the fragment 2 region during activation in the presence of factor V’, Journal of Biological Chemistry, 249, 7791–7Google Scholar
  111. Esmon, CT., Stenflo, J., Suttie, J.W. and Jackson, CM. (1976) ‘A new vitamin K-dependent protein: A phospholipid-binding zymogen of a serine esterase’, Journal of Biological Chemistry, 251, 3052–6Google Scholar
  112. Esmon, N.L., Owen, W.G. and Esmon, C.T. (1982) ‘Isolation of a membrane-bound cofactor for thrombin-catalyzed activation of protein C’, Journal of Biological Chemistry, 257, 859–64Google Scholar
  113. Fair, B.D., Saito, H., Ratnoff, O.D. and Rippon, W.B. (1977) ‘Detection by fluorescence of structural changes accompanying the activation of Hageman factor (factor XII)’, Proceedings of the Society for Experimental Biology and Medicine, 155, 199–202Google Scholar
  114. Fass, D.N., Knutson, G.J. and Bowie, E.J.W. (1978) ‘Porcine Willebrand factor: a population of multimer’, Journal of Laboratory and Clinical Medicine, 91, 307–20Google Scholar
  115. von Felton, A. and Straub, P.W. (1969) ‘Coagulation studies of cord blood, with special reference to “fetal fibrinogen’”, Thrombosis et Diathesis Haemorrhagica, 22, 273–80Google Scholar
  116. Fenton, J.W., Fasco, M.J., Stackrow, A.B., Aronson, D.L., Young, A.M. and Finlayson, J.S. (1977) ‘Human thrombins. Production, evaluation and properties of a-thrombin’, Journal of Biological Chemistry, 252, 3587–98Google Scholar
  117. Ferry, J.D. (1952) ‘The mechanism of polymerization of fibrin’, Proceedings of the National Academy of Sciences, 38, 566–9CrossRefGoogle Scholar
  118. Fish, W. and Björk, I. (1979a) ‘Production by thrombin of a proteolytically modified form of antithrombin and release of the same form from the antithrombin-thrombin complex’, Thrombosis and Haemostasis, 42, 129Google Scholar
  119. Fish, W.W. and Bjprk, I. (1979b) ‘Release of a two-chain form of antithrombin from the antithrombin-thrombin complex’, European Journal of Biochemistry, 101, 31–8CrossRefGoogle Scholar
  120. Forbes, CD., Pensky, J. and Ratnoff, O.D. (1970) ‘Inhibition of activated Hageman factor and activated plasma thromboplastin antecedent by purified CI inactivator’, Journal of Laboratory and Clinical Medicine, 76, 809–15Google Scholar
  121. Fowler, W.E. and Erickson, H.P. (1979) ‘The trinodular structure of fibrinogen: confirmation by both shadowing and negative stain electron microscopy’, Journal of Molecular Biology, 134, 241–9CrossRefGoogle Scholar
  122. Fowler, W.E., Fretto, L.J., Erickson, H.P. and McKee, P.A. (1980) ‘Electron microscopy of plasmic fragments of human fibrinogen as related to trinodular structure of the intact molecule’, Journal of Clinical Investigation, 66, 50–6CrossRefGoogle Scholar
  123. Franks, J.J., Kirsch, R.E., Frith, L.O., Purves, I.R., Franks, W.T., Franks, J.A., Mason, P. and Saunders, S.J. (1981) ‘Effect of fibrinogenolytic products D and E on fibrinogen and albumin synthesis in the rat’, Journal of Clinical Investigation, 67, 575–80CrossRefGoogle Scholar
  124. Franzen, L.-E., Svensson, S. and Larm, O. (1980) ‘Structural studies on the carbohydrate portion of human antithrombin IIP’, Journal of Biological Chemistry, 255, 5090–3Google Scholar
  125. Fretto, L.J., Ferguson, E.W., Steinman, H.M. and McKee, P.A. (1978) ‘Localization of the a-chain cross-link acceptor sites of human fibrin’, Journal of Biological Chemistry, 253, 2184–95Google Scholar
  126. Fryklund, L., Borg, H. and Andersson, L.-O. (1976) ‘Amino-terminal sequence of human factor IX: presence of y-carboxyl glutamic acid residues’, FEBS Letters, 65, 187–9CrossRefGoogle Scholar
  127. Fujikawa, K., Legaz, M.E. and Davie, E.W. (1972) ‘Bovine factors X x and X2 (Stuart factor). Isolation and characterization’, Biochemistry, 11, 4882–91CrossRefGoogle Scholar
  128. Fujikawa, K., Thompson, A.R., Legaz, M.E., Meyer, R.G. and Davie, E.W. (1973) ‘Isolation and characterization of bovine factor IX (Christmas factor)’, Biochemistry, 12, 4938–45CrossRefGoogle Scholar
  129. Fujikawa, K., Coan, M.H., Legaz, M.E. and Davie, E.W. (1974a) ‘The mechanism of activation of bovine factor X (Stuart factor) by intrinsic and extrinsic pathways’, Biochemistry, 13, 5290–9CrossRefGoogle Scholar
  130. Fujikawa, K., Legaz, M.E., Kato, H. and Davie, E.W. (1974b) ‘The mechanism of activation of bovine factor IX (Christmas factor) by bovine factor Xla (activated plasma thromboplastin antecedent)’ Biochemistry, 13, 4508–16CrossRefGoogle Scholar
  131. Fujikawa, K., Walsh, K.A. and Davie, E.W. (1977a) ‘Isolation and characterization of bovine factor XII (Hageman factor)’, Biochemistry, 16, 2270–8CrossRefGoogle Scholar
  132. Fujikawa, K., Kurachi, K. and Davie, E.W. (1977b) ‘Characterization of bovine factor Xlla (activated Hageman factor)’, Biochemistry, 16, 4182–8CrossRefGoogle Scholar
  133. Fujikawa, K., Heimark, R.L., Kurachi, K. and Davie, E.W. (1980) ‘Activation of bovine factor XII (Hageman factor) by plasma kallikrein’, Biochemistry, 19, 1322–30CrossRefGoogle Scholar
  134. Fuller, G.M. and Ritchie, D.G. (1981) ‘A regulatory pathway for fibrinogen biosynthesis involving an indirect feedback loop’, Annals of the New York Academy of Sciences, 389, 308–22CrossRefGoogle Scholar
  135. Gaffney, P.J. (1972) ‘Localisation of carbohydrate in the subunits of human fibrinogen and its plasmin-induced fragments’, Biochimica et Biophysica Acta, 263, 453–8Google Scholar
  136. Galanakis, D.R. and Mosesson, M.W. (1977) ‘Comparative studies on fetal fibrinogen from full term and premature infants’, Thrombosis and Haemostasis, 38, 102Google Scholar
  137. Galanakis, D.R. and Mosesson, M.W, (1979) ‘Correction of the delayed fibrin aggregation of fetal fibrinogen by partial removal of sialic acid’, Thrombosis and Haemostasis, 42, 79Google Scholar
  138. Gallimore, M.J., Fareid, E. and Stormorken, H. (1978) ‘The purification of human plasma kallikrein with weak plasminogen activator activity’, Thrombosis Research, 12, 409–20CrossRefGoogle Scholar
  139. Gallimore, M.J., Amundsen, E., Larsbraaten, M., Lyngaas, K. and Fareid, E. (1979) ‘Studies on plasma inhibitors of plasma kallikrein using chromogenic peptide substrate assays’, Thrombosis Research, 16, 695–703CrossRefGoogle Scholar
  140. Gallin, J.I. and Kaplan, A.P. (1974) ‘Mononuclear cell chemotactic activity of kallikrein and plasminogen activator and its inhibition by CI inhibitor and a2-macroglobulin’, Journal of Immunology, 113,1928–34Google Scholar
  141. Ganrot, P.O. and Nilehn, J.E. (1968) ‘Plasma prothrombin during treatment with Dicoumarol II. Demonstration of an abnormal prothrombin fraction’, Scandinavian Journal of Clinical and Laboratory Investigation, 22, 27–8CrossRefGoogle Scholar
  142. Gans, H. and Tan, B.H. (1967) ‘A antitrypsin, an inhibitor for thrombin and plasmin’, Clinica Chimica Acta, 17, 111–117CrossRefGoogle Scholar
  143. Gedde-Dahl, T.W., Jeremic, M. and Weisert, O. (1975) ‘Factor V (proaccelerin) concentration in 1016 blood donors. The effects of age, sex, and ABO blood groups’, Scandinavian Journal of Clinical and Laboratory Investigation, 35, 25–30CrossRefGoogle Scholar
  144. Giddings, J.C, Shearn, S.A.M. and Bloom, A.L. (1975) ‘The immunological localization of factor V in human tissue’, British Journal of Haematology, 29, 57–65CrossRefGoogle Scholar
  145. Gigli, I., Mason, J.W., Colman, R.W. and Austen, K.F. (1970) ‘Interaction of plasma kallikrein with CI-inactivator’, Journal of Immunology, 104, 574–81Google Scholar
  146. Ginsberg, M.H., Jaques, B., Cochrane, CG. and Griffin, J.H. (1980) ‘Urate crystal-dependent cleavage of Hageman factor in human plasma and in synovial fluid’, Journal of Laboratory and Clinical Medicine, 95, 497–506Google Scholar
  147. Gjonnaess, H. (1972) ‘Cold promoted activation of factor VIII. I. Evidence for the existence of an activator’, Thrombosis et Diathesis Haemorrhagica, 28, 155–68Google Scholar
  148. Godal, H.C, Rygh, M. and Laake, K. (1974) ‘Progressive inactivation of purified factor VII by heparin and antithrombin IIP’, Thrombosis Research, 5, 773–5CrossRefGoogle Scholar
  149. Green, A.J. and Ratnoff, O.D. (1974) ‘Elevated antihemophilic factor (AHF, factor VIII) procoagulant activity and AHF-like antigen in alcoholic cirrhosis of the liver’, Journal of Laboratory and Clinical Medicine, 83, 189–97Google Scholar
  150. Greenberg, CS. and Shulman, M.A, (1982) ‘The zymogen forms of blood coagulation factor XII binds specifically to fibrinogen’, Journal of Biological Chemistry, 257, 6096–101Google Scholar
  151. Griffin, J.H. (1977) ‘New hypothesis for the molecular mechanism of surface-dependent activation of Hageman factor (factor XII)’, Thrombosis and Haemostasis, 38, 50Google Scholar
  152. Griffin, J.H. and Cochrane, CG. (1976) ‘Mechanisms for the involvement of high molecular weight kininogen in surface-dependent reactions of Hageman factor’, Proceedings of the National Academy of Sciences, 73, 2554–8CrossRefGoogle Scholar
  153. Guillin, M.-C. and Menache, D. (1973) ‘Fetal fibrinogen and fibrinogen Paris I: comparative fibrin monomers aggregation studies’, Thrombosis Research, 3, 117–35CrossRefGoogle Scholar
  154. Hall, C and Slayter, H. (1959) ‘The fibrinogen molecule: its size, shape, and mode of polymerization’, Journal of Biophysical and Biochemical Cytology, 5, 11–5CrossRefGoogle Scholar
  155. Han, Y.N., Komiya, M., Iwanaga, S. and Suzukui, Y. (1975a) ‘Studies on the primary structure of bovine high-molecular weight kininogen. Amino acid sequence of a fragment (“Histidine-rich peptide”) released by plasma kallikrein’, Journal of Biochemistry, 77, 55–68Google Scholar
  156. Han, Y.N., Komiya, M., Kato, H., Iwanaga, S. and Suzuki, T. (1975b) ‘Primary structure of bovine high molecular weight kininogen: chemical compositions of kinin-free kininogen and peptide fragments released by plasma kallikrein’, FEBS Letters’, 57,254–8CrossRefGoogle Scholar
  157. Han, Y.N., Kato, H., Iwanaga, S. and Suzuki, T. (1976) ‘Bovine plasma high molecular weight kininogen: the amino acid sequence of fragment 1 (glycopeptide) released by the action of plasma kallikrein and its location in the precursor protein’, FEBS Letters, 63, 197–200CrossRefGoogle Scholar
  158. Harmon, J., Jamieson, G.A. and Rock, G. (1981) ‘Determination of molecular size of VIILC in whole plasma by electron irradiation’, Thrombosis and Haemostasis, 46, 255Google Scholar
  159. Harpel, P.C,. (1970) ‘Human plasma alpha2-macroglobulin. An inhibitor of plasma kallikrein’, Journal of Experimental Medicine, 132, 329–52CrossRefGoogle Scholar
  160. Harpel, P.C. (1972) ‘Studies on the interaction between collagen and a plasma kallikrein-like activity. Evidence for a surface-active enzyme system’, Journal of Clinical Investigation, 51, 1813–22CrossRefGoogle Scholar
  161. Harpel, P.C. (1973) ‘Studies on human plasma a2-macroglobulin-enzyme interactions’, Journal of Experimental Medicine, 138, 508–21CrossRefGoogle Scholar
  162. Hathaway, W.E., Beihasen, L.P. and Hathaway, H.S. (1965) ‘Evidence for a new thromboplastin factor: Case report, coagulation studies and physicochemical studies’, Blood, 26, 521–32Google Scholar
  163. Hatton, M.W.C., Berry, L.R. and Regoeczi, E. (1978) ‘Inhibition of thrombin by antithrombin III in the presence of certain glycosaminoglycans found in the mammalian aorta’, Thrombosis Research, 13, 655–70CrossRefGoogle Scholar
  164. Heber, H., Geiger, R. and Heimburger, N. (1978) ‘Human plasma kallikrein: purification, enzyme characterization and quantitative determination in plasma’, Hoppe-Seyler’s Zeitschrift fur Physiologische Chemie, 359, 659–69Google Scholar
  165. Heck, L.W. and Kaplan, A.P. (1974) ‘Substrates of Hageman factor. I. Isolation and characterization of human factor XI (PTA) and inhibition of the activated enzyme by a,-antitrypsin’, Journal of Experimental Medicine, 140, 1615–30CrossRefGoogle Scholar
  166. Hedner, U. (1979) ‘Inhibition of Hageman factor by a fibrinolytic inhibitor’, Thrombosis and Haemostasis, 42, 262Google Scholar
  167. Hedner, U. and Martinsson, G. (1978) ‘Inhibition of activated Hageman factor (factor Xlla) by an inhibitor of the plasminogen activation (PA inhibitor)’, Thrombosis Research, 12, 1015–23CrossRefGoogle Scholar
  168. Heimark, R.L. and Davie, E.W. (1979) ‘Isolation and characterization of bovine plasma prekallikrein (Fletcher factor)’, Biochemistry, 18, 5743–50CrossRefGoogle Scholar
  169. Heimark, R.L., Kurachi, K., Fujikawa, K. and Davie, E.W. (1980) ‘Surface activation of blood coagulation, fibrinolysis and kinin formation’, Nature, 286, 456–60CrossRefGoogle Scholar
  170. Heimburger, N., Haupt, H. and Schwick, H.G. (1971) ‘Proteinase inhibitors of human plasma’, in H. Fritz and H. Tschesche (eds.) Proceedings of the International Research Conference on Proteinase Inhibitors, Walter de Gruyter, Berlin and New York, pp. 1–22Google Scholar
  171. Hemker, H.C. and Muller, A.D. (1968) ‘Kinetic aspects of the interaction of blood-clotting enzymes. VI. Localization of the site of blood-coagulation inhibition by the protein induced by vitamin K absence (PIVKA)’, Thrombosis et Diathesis Haemorrhagica, 20, 78–87Google Scholar
  172. Hemker, H.C, Veitkamp, J.J., Hensen, A. and Loeliger, E.A. (1963) ‘Nature of prothrombin biosynthesis: preprothrombinaemia in vitamin K-deficiency’, Nature, 200, 589–90CrossRefGoogle Scholar
  173. Henschen, A. and Lottspeich, F. (1977) ‘Amino acid sequence of human fibrin. Preliminary note on the completion of the ß chain sequence’, Hoppe-Seyler’s Zeitschrift fur Physiologische Chemie, 358, 1643–6Google Scholar
  174. Hessel, B., Makino, M., Iwanaga, S. and Blombäck, B. (1979) ‘Primary structure of human fibrinogen and fibrin. Structural studies on NH2-terminal part of Bß chain’, European Journal of Biochemistry, 98, 521–34CrossRefGoogle Scholar
  175. Hjort, P., Rapaport, S.I. and Owren, P.A. (1955) ‘Evidence that platelet accelerator (platelet factor I) is adsorbed plasma proaccelerin’, Blood, 10, 1139–50Google Scholar
  176. Hojrup, P., Roepstorff, P. and Petersen, T.E. (1982) ‘Amino-acid sequence of the vitamin-K-dependent part of protein Z’, European Journal of Biochemistry, 126, 343–8CrossRefGoogle Scholar
  177. Holmer, E., Söderström, G. and Andersson, L.-O. (1979) ‘Studies on the mechanism of the rate-enhancing effect of heparin on the thrombin- antithrombin III reaction’, European Journal of Biochemistry, 93, 1–5CrossRefGoogle Scholar
  178. Höök, C, Björk, I., Hopwood, J. and Lindahl, U. (1976) ‘Anticoagulant activity of heparin: separation of high-activity and low-activity heparin species by affinity chromatography on immobilised antithrombin’, FEBS Letters, 66, 90–3CrossRefGoogle Scholar
  179. Hopwood, J., Höök, M., Linker, A. and Lindahl, U. (1976) ‘Anticoagulant activity of heparin: isolation of antithrombin-binding sites’, FEBS Letters, 69, 51–4CrossRefGoogle Scholar
  180. Horowitz, H.I. and Fujimoto, M.M. (1965) ‘Association of factors XI and XII with blood platelets’, Proceedings of the Society for Experimental Biology and Medicine, 779,487–92Google Scholar
  181. Hougie, C, Denson, K.W. and Biggs, R. (1967) ‘A study of the reaction product of factor VIII and factor IX by gel filtration’, Thrombosis et Diathesis Haemorrhagica, 18, 211–22Google Scholar
  182. Howard, J.B. and Nelsestuen, G.L. (1975) ‘Isolation and characterization of vitamin K-dependent region of bovine clotting factor X’, Proceedings of the National Academy of Sciences, 72, 1281–1285CrossRefGoogle Scholar
  183. Hoyer, L.W. and Trabold, N.C. (1981) ‘The effect of thrombin on human factor VIII. Cleavage of the factor VIII procoagulant protein during activation’, Journal of Laboratory and Clinical Medicine, 97, 50–64Google Scholar
  184. Hultin, M.B. and Nemerson, Y. (1978) ‘Activation of factor X by factors IXa and VIII; a specific assay for factor IXa in the presence of thrombin-activated factor VIII’, Blood, 52, 928–40Google Scholar
  185. Hurst, R.E., Menter, J.M., West, S.S., Settine, J.M. and Coyne, E.H. (1979) ‘Structural basis for the anticoagulant activity of heparin. I. Relationship to the number of charged groups’, Biochemistry, 18, 4283–7CrossRefGoogle Scholar
  186. Hvatum, M. and Prydz, H. (1969) ‘Studies on tissue thromboplastin — its splitting into two separable parts’, Thrombosis et Diathesis Haemorrhagica, 21, 217–22Google Scholar
  187. Ikari, N., Sugo, T., Fujii, S. and Iwanaga, S. (1981) ‘The role of bovine high-molecular weight (HMW) kininogen in contact-mediated activation of bovine factor XII: interaction of HMW kininogen with kaolin and plasma prekallikrein’, Journal of Biochemistry, 89, 1699–709Google Scholar
  188. Ittyerah, T.R., Weidner, N., Wochner, R.D. and Sherman, L.A. (1979) ‘Effect of fibrin degradation products and thrombin on fibrinogen synthesis’, British Journal of Haematology, 43, 661–8CrossRefGoogle Scholar
  189. Iwamoto, M. and Abiko, Y. (1970) ‘Plasminogen-plasmin system. VI. Preparation of a2-macroglobulin antiplasmin from human plasma’, Biochimica et Biophysica Acta, 214, 402–10Google Scholar
  190. Jackson, CM. (1972) ‘Characterisation of two glycoprotein variants of bovine factor X and demonstration that the factor X zymogen contains two polypeptide chains’, Biochemistry, 11, 4873–81CrossRefGoogle Scholar
  191. Jackson, CM. and Hanahan, D.J. (1968) ‘Studies on bovine factor X. II. Observations on some alterations in zone electrophoretic and chromatographic behavior occurring during purification’, Biochemistry, 7, 4506–17CrossRefGoogle Scholar
  192. Jaffe, E.A. and Nachman, R.L. (1975) ‘Subunit structure of factor VIII antigen synthesized by cultured human endothelial cells’, Journal of Clinical Investigation, 56, 698–702CrossRefGoogle Scholar
  193. Jaffe, E.A., Hoyer, L.W. and Nachman, R.L. (1973) ‘Synthesis of antihemophilic factor antigen by cultured human endothelial cells’, Journal of Clinical Investigation, 52, 2757–64CrossRefGoogle Scholar
  194. Jaffe, E.A., Hoyer, L.W. and Nachman, R.L. (1974) ‘Synthesis of von Willebrand factor by cultured human endothelial cells’, Proceedings of the National Academy of Sciences, 71, 1906–9CrossRefGoogle Scholar
  195. Jeejeebhoy, K.N., Bruce-Robertson, A., Sodtke, U. and Foley, M. (1970) ‘The effect of growth hormone on fibrinogen synthesis’, Biochemical Journal, 119, 243–9Google Scholar
  196. Jeejeebhoy, K.N., Ho, J., Greenberg, G.R., Phillips, M.J., Bruce-Robertson, A. and Sodtke, U. (1975) ‘Albumin, fibrinogen and transferrin synthesis in isolated rat hepatocyte suspensions’, Biochemical Journal, 146, 141–55Google Scholar
  197. Jesty, J. (1978) ‘The inhibition of activated bovine coagulation factors X and VII by antithrombin IIP’, Archives of Biochemistry and Biophysics, 185, 165–73CrossRefGoogle Scholar
  198. Jesty, J. (1979) ‘Dissociation of complexes and their derivatives formed during inhibition of bovine thrombin and activated factor X by antithrombin IIP’, Journal of Biological Chemistry, 254, 1044–9Google Scholar
  199. Jesty, J. and Nemerson, Y. (1974) ‘Purification of factor VII from bovine plasma. Reaction with tissue factor and activation of factor X’, Journal of Biological Chemistry, 249, 509–15Google Scholar
  200. Jesty, J. and Silverberg, S.A. (1979) ‘Kinetics of the tissue factor-dependent activation of coagulation factors IX and X in a bovine plasma system’, Journal of Biological Chemistry, 254, 12337–45Google Scholar
  201. Jesty, J., Spencer, A.K. and Nemerson, Y. (1974) ‘The mechanism of activation of factor X. Kinetic control of alternative pathways leading to the formation of activated factor X’, Journal of Biological Chemistry, 249, 5614–22Google Scholar
  202. Jesty, J., Spencer, A.K., Nakashima, Y., Nemerson, Y and Königsberg, W. (1975) ‘The activation of coagulation factor X. Identity of cleavage sites in the alternative activation pathways and characterization of the COOH-terminal peptide’, Journal of Biological Chemistry, 250, 4497–504Google Scholar
  203. Johnson, E.A. and Mulloy, B. (1976) ‘The molecular weight range of mucosal heparins’, Carbohydrate Research, 1951, 119–127CrossRefGoogle Scholar
  204. Jones, J.M., Creeth, J.M. and Kekwick, R.A. (1972) ‘Thiol reduction of human a2-macroglobulin. The subunit structure’, Biochemical Journal, 127, 187–97Google Scholar
  205. Jordan, R., Beeler, D. and Rosenberg, R. (1979) ‘Fractionation of low molecular weight heparin species and their interaction with antithrombin’, Journal of Biological Chemistry, 254, 2902–13Google Scholar
  206. Jordan, R.E., Favreau, L.V., Braswell, E.H. and Rosenberg, R.D. (1982) ‘Heparin with two binding sites for antithrombin or platelet factor 4’, Journal of Biological Chemistry, 257, 400–6Google Scholar
  207. Josso, F. and Beguin, S. (1981) ‘Changes in the antithrombin III activity at the interface plasma-phospholipids’, Thrombosis and Haemostasis, 46, 285Google Scholar
  208. Kalousek, F., Königsberg, W. and Nemerson, Y. (1975) ‘Activation of factor IX by activated factor X: a link between the extrinsic and intrinsic coagulation systems’, FEBS Letters, 50, 382–5Google Scholar
  209. Kampschmidt, R.F. and Upchurch, H.F. (1974) ‘Effect of leucocyte endogenous mediator on plasma fibrinogen and haptoglobin’, Proceedings of the Society for Experimental Biology and Medicine, 146, 904–7Google Scholar
  210. Kampschmidt, R.F., Upchurch, H.F. and Pulliam, L.A. (1981) ‘Characterization of a leukocyte-derived endogenous mediator responsible for increased plasma fibrinogen’, Annals of the New York Academy of Sciences, 389, 338–51CrossRefGoogle Scholar
  211. Kane, W.H., Lindhout, M.J., Jackson, CM. and Majerus, P.W. (1980) ‘Factor Va-dependent binding of factor Xa to human platelets’, Journal of Biological Chemistry, 255, 1170–4Google Scholar
  212. Kato, H., Sugo, T., Ikari, N., Hashimoto, N., Iwanaga, S. and Fujii, S. (1979) ‘Role of bovine HMW in kininogen in contact-mediated activation of factor XII: Demonstration of a nicked form, “active kininogen”, with maximal co-factor activity by limited proteolysis’, Thrombosis and Haemostasis, 42, 262Google Scholar
  213. Kerbiriou, D.M. and Griffin, J.H. (1979) ‘Human high molecular weight kininogen. Studies of structure-function relationships and of proteolysis of the molecule occurring during contact activation of plasma’, Journal of Biological Chemistry, 254, 12020–7Google Scholar
  214. Kerbiriou, D.H., Bouma, B.N. and Griffin, J.H. (1980) ‘Immunochemical studies of human high molecular weight kininogen and of its complexes with plasma prekallikrein or kallikrein’, Journal of Biological Chemistry, 255, 3952–8Google Scholar
  215. Kessler, CM. and Bell, W.R. (1979a) ‘Regulation of fibrinogen biosynthesis: effect of fibrin degradation products, low-molecular-weight peptides of fibrinogenolysis, and fibrinopeptides A and B’, Journal of Laboratory and Clinical Medicine, 93, 758–67Google Scholar
  216. Kessler, CM. and Bell, W.R. (1979b) ‘The effect of homologous thrombin and fibrinogen degradation products on fibrinogen synthesis in rabbits’, Journal of Laboratory and Clinical Medicine, 93, 768–82Google Scholar
  217. Kiesselbach, T.H. and Wagner, R.H. (1972) ‘Demonstration of factor XIII in human megakaryocytes by a fluorescent antibody technique’, Annals of the New York Academy of Sciences, 202, 318–28CrossRefGoogle Scholar
  218. Kisiel, W. (1979) ‘Human plasma protein C. Isolation, characterization, and mechanism of activation by a-thrombin’, Journal of Clinical Investigation, 64, 761–9CrossRefGoogle Scholar
  219. Kisiel, W. and Davie, E.W. (1975) ‘Isolation and characterization of bovine factor VII’, Biochemistry, 14, 4928–34CrossRefGoogle Scholar
  220. Kisiel, W. and McMullen, B.A. (1981) ‘Isolation and characterization of human factor Vila’, Thrombosis Research, 22, 375–80CrossRefGoogle Scholar
  221. Kisiel, W., Ericsson, L.H. and Davie, E.W. (1976) ‘Proteolytic activation of protein C from bovine plasma’, Biochemistry, 15, 4893–900CrossRefGoogle Scholar
  222. Kisiel, W., Fujikawa, K. and Davie, E.W. (1977a) ‘Activation of bovine factor VII (proconvertin) by factor Xlla (activated Hageman factor)’, Biochemistry, 16, 4189–94CrossRefGoogle Scholar
  223. Kisiel, W., Canfield, W.M., Ericsson, L.H. and Davie, E.W. (1977b) ‘Anticoagulant properties of bovine plasma protein C following activation by thrombin’, Biochemistry, 16, 5824–31CrossRefGoogle Scholar
  224. Koide, T. (1979) ‘Isolation and characterization of antithrombin III from human, porcine and rabbit plasma, and rat serum’, Journal of Biochemistry, 86, 1841–50Google Scholar
  225. Koide, T., Kato, H. and Davie, E.W. (1977) ‘Isolation and characterization of bovine factor XI (plasma thromboplastin antecedent)’, Biochemistry, 16, 2279–86CrossRefGoogle Scholar
  226. Koide, T., Odani, S. and Ono, T. (1982) ‘The N-terminal sequence of human plasma histidine-rich glycoprotein homologous to antithrombin with high affinity for heparin’, FEBS Letters, 141, 222–4CrossRefGoogle Scholar
  227. Komiya, M., Kato, H. and Suzuki, T. (1974) ‘Bovine plasma kininogens I. Further purification of high molecular weight kininogen and its physicochemical Properties’, Journal of Biochemistry, 76, 811–22Google Scholar
  228. Kosow, D.P. and Orthner, CL. (1979) ‘Kinetics of the activation of human prothrombin by human coagulation factor Xa. Initial rate studies in the presence of Ca2+ and phospholipid’, Journal of Biological Chemistry, 254, 9448–52Google Scholar
  229. Koutts, J., Walsh, P.N., Plow, E.F., Fenton, J.W., Bouma, B.N. and Zimmerman, T.S. (1978) ‘Active release of human platelet factor VIH-related antigen by adenosine diphosphate, collagen, and thrombin’, Journal of Clinical Investigation, 62, 1255–63CrossRefGoogle Scholar
  230. Kraemer, P.M. (1977) ‘Heparin releases heparan sulphate from the cell surface’, Biochemical and Biophysical Research Communications, 78, 1334–40CrossRefGoogle Scholar
  231. Kropatkin, M.L. and Izak, G. (1968) ‘Studies on the hypercoagulable state’, Thrombosis et Diathesis Haemorrhagica, 19, 547–55Google Scholar
  232. Kudryk, B.J., Collen, D., Woods, K.R. and Blombäck, B. (1974) ‘Evidence for localization of polymerization sites in fibrinogen’, Journal of Biological Chemistry, 249, 3322–5Google Scholar
  233. Kueppers, F. and Fallat, R.J. (1969) ‘A -antitrypsin deficiency: a defect in protein synthesis’, Clinica Chimica Acta, 24, 401–3CrossRefGoogle Scholar
  234. Kurachi, K. and Davie, E.W, (1977) ‘Activation of human factor XI (plasma thromboplastin antecedent) by factor Xlla (activated Hageman factor)’, Biochemistry, 16, 5831–9CrossRefGoogle Scholar
  235. Kurachi, K., Schmer, G., Herodson, M.A., Teller, D.C. and Davie, E.W. (1976a) ‘Characterization of human, bovine, and horse antithrombin III’, Biochemistry, 15, 368–73CrossRefGoogle Scholar
  236. Kurachi, K., Fujikawa, K., Schmer, G. and Davie, E.W. (1976b) ‘Inhibition of bovine factor IXa and factor Xaß by antithrombin III’, Biochemistry, 15, 373–7CrossRefGoogle Scholar
  237. Kurachi, K., Fujikawa, K. and Davie, E.W. (1980) ‘Mechanism of activation of bovine factor XI by factor XII and factor Xlla’, Biochemistry, 19, 1330–8CrossRefGoogle Scholar
  238. Laake, K. and Ellingsen, R. (1974) ‘Purification and some characteristics of factor VII in human citrated plasma, glass-activated serum, and cold-activated plasma’, Thrombosis Research, 5, 539–56CrossRefGoogle Scholar
  239. Laake, K. and Osterud, B. (1974) ‘Activation of purified plasma VII by human plasmin, plasma kallikrein, and activated components of the human intrinsic blood coagulation system’, Thrombosis Research, 5, 759–72CrossRefGoogle Scholar
  240. Laki, K. and Gladner, J.A. (1964) ‘Chemistry and physiology of the fibrinogen-fibrin transition’, Physiological Reviews, 44, 127–60Google Scholar
  241. Lanchantin, G.F., Plesset, M.L., Friedmann, J.A. and Hart, D.W. (1966) ‘Dissociation of esterolytic and clotting activities of thrombin by trypsin-binding macroglobulin’, Proceedings of the Society of Experimental Biology and Medicine, 121, 444–9Google Scholar
  242. Lane, J.L., Bird, P. and Rizza, C.R. (1975) ‘A new assay for the measurement of total progressive antithrombin’, British Journal of Haematology, 30, 103–115CrossRefGoogle Scholar
  243. Larrieu, M.J., Soulier, J.P. and Minkowski, A. (1952) ‘Le sang du cordon ombilical: Etude complete de sa coagulability, comparison avec le sang maternal’, Etudes Neonatales, 1, 39–60Google Scholar
  244. Larrieu, M.J., Rigollot, C. and Marder, V.J. (1972) ‘Comparative effects of fibrinogen degradation fragments D and E on coagulation’, British Journal of Haematology, 22, 719–33CrossRefGoogle Scholar
  245. Larrieu, M.J., Dray, L. and Ardaillou, N. (1975) ‘Biological effects of fibrinogen-fibrin degradation products’, Thrombosis et Diatheses Haemorrhagica, 34, 686–92Google Scholar
  246. Latallo, Z.S., Budzynski, A.Z., Lipinski, B. and Kowalski, E. (1964) ‘Inhibition of thrombin and of fibrin polymerization, two activities derived from plasmin- digested fibrinogen’, Nature, 203, 1184–5CrossRefGoogle Scholar
  247. Lau, H.K. and Rosenberg, R.D. (1980) ‘The isolation and characterization of a specific antibody population directed against tne thrombin-antithrombin complex’, Journal of Biological Chemistry, 255, 5885–93Google Scholar
  248. Laudano, A.P. and Doolittle, R.F. (1978) ‘Synthetic peptide derivatives that bind to fibrinogen and prevent the polymerization of fibrin monomers’, Proceedings of the National Academy of Sciences, 75, 3085–9CrossRefGoogle Scholar
  249. Laudano, A.P. and Doolittle, R.F. (1980) ‘Studies on synthetic peptides that bind to fibrinogen and prevent fibrin polymerization. Structural requirements, number of binding sites, and species differences’, Biochemistry, 19, 1013–1019CrossRefGoogle Scholar
  250. Laurent, T.C. and Blombäck, B. (1958) ‘On the significance of the release of two different peptides from fibrinogen during clotting’, Acta Chemica Scandinavica, 12, 137–46CrossRefGoogle Scholar
  251. Laurent, T.C, Tengblad, A., Thunberg, L., Höök, M. and Lindahl, U. (1978) ‘On the molecular weight dependence of the anticoagulant activity of heparin’, Biochemical Journal, 175, 691–701Google Scholar
  252. Learned, L.A., Bloom, J.W. and Hunter, M.J. (1976) ‘The antithrombin activity of a-1-protease inhibitor: the antitrypsin activity of antithrombin III’, Thrombosis Research, 8, 99–109CrossRefGoogle Scholar
  253. Lee, A.K.Y., Chan, V. and Chan, T.K. (1979) ‘The identification and localization of antithrombin III in human tissues’, Thrombosis Research, 14, 209–17CrossRefGoogle Scholar
  254. Lee, S.Y. and Chung, S.I. (1976) ‘Biosynthesis and degradation of plasma protransglutaminase (factor XIII)’, Federation Proceedings, 35, 1486Google Scholar
  255. Legaz, M.E., Schmer, G., Counts, R.B. and Davie, E.W. (1973) ‘Isolation and characterization of human factor VIII (antihemophilic factor)’, Journal of Biological Chemistry, 248, 3946–55Google Scholar
  256. Liang, T.J. and Grieninger, G. (1981) ‘Direct effect of insulin on the synthesis of specific plasma proteins: Biphasic response of hepatocytes cultured in serum- and hormone-free medium’, Proceedings of the National Academy of Sciences, 78, 6972–6CrossRefGoogle Scholar
  257. Lindahl, U., Bäckström, G., Höök, M., Thunberg, L., Fransson, L.-A. and Linker, A. (1979) ‘Structure of the antithrombin-binding site in heparin’, Proceedings of the National Academy of Sciences, 76, 3198–202CrossRefGoogle Scholar
  258. Link, K.P. (1959) ‘The discovery of dicumarol and its sequels’, Circulation, 19, 97–107Google Scholar
  259. Lipscomb, M.S. and Walsh, P.N. (1979) ‘Human platelets and factor XI. Localization in platelet membranes of factor XI-like activity and its functional distinction from plasma factor XI’, Journal of Clinical Investigation, 63, 1006–14CrossRefGoogle Scholar
  260. Liu, D.T.H. and McCoy, L.E. (1975) ‘Tissue extract thromboplastin: Quantitation, fractionation and characterization of protein components’, Thrombosis Research, 7, 199–211CrossRefGoogle Scholar
  261. Lollar, P., Hoak, T.C. and Owen, W.G. (1980) ‘Binding of thrombin to cultured human endothelial cells. Nonequilibrium aspects’, Journal of Biological Chemistry, 255, 10279–83Google Scholar
  262. Loskutoff, D.J. (1979) ‘Effect of thrombin on the fibrinolytic activity of cultured bovine endothelial cells’, Journal of Clinical Investigation, 64, 329–32CrossRefGoogle Scholar
  263. Losowsky, M.S. and Walls, W.D. (1979) ‘Mechanisms of acquired defects of the stabilization of fibrin’, British Journal of Haematology, 20, 377–83CrossRefGoogle Scholar
  264. Lottspeich, F. and Henschen, A. (1977a) ‘Amino acid sequence of human fibrin. Preliminary note on the completion of the y-chain sequence’, Hoppe-Seyler’s Zeitschrift fur Physiologische Chemie, 358, 935–8Google Scholar
  265. Lottspeich, F. and Henschen, A. (1977b) ‘Amino acid sequence of human fibrin. Preliminary note on three internal peptides obtained by cyanogen bromide cleavage of the ß-chain’, Hoppe-Seyler’s Zeitschrift fur Physiologische Chemie, 358, 1639–42CrossRefGoogle Scholar
  266. Lundblad, R.L., Noyes, CM., Mann, K.G. and Kingdon, H.S. (1979) ‘The covalent differences between bovine a- and ß-thrombin’, Journal of Biological Chemistry, 254, 8524–8Google Scholar
  267. Lutcher, CL. (1976) ‘Reid trait: A new expression of high molecular weight kininogen (HMW kininogen) deficiency’, Clinical Research, 24, 47Google Scholar
  268. MacGregor, I.R., Lane, D.A. and Kakkar, V.V. (1979) ‘Evidence for a plasma inhibitor of the heparin accelerated inhibition of factor Xa by antithrombin IIP’, Biochimica et Biophysica Acta, 586, 584–93CrossRefGoogle Scholar
  269. Machovich, R. (1975) ‘Mechanism of action of heparin through thrombin on blood coagulation’, Biochimica et Biophysica Acta, 412, 13–7Google Scholar
  270. Machovich, R., Blasko, G. and Palos, L.A. (1975) ‘Action of heparin on thrombin-antithrombin reaction’, Biochimica et Biophysica Acta, 379, 193–200Google Scholar
  271. Mackie, M., Bennett, B., Ogston, D. and Douglas, A.S. (1978) ‘Familial thrombosis: inherited deficiency of antithrombin IIP’, British Medical Journal, 1, 136–8CrossRefGoogle Scholar
  272. Magnusson, S., Sottrup-Jensen, L. and Petersen, T.E. (1974) ‘Primary structure of the vitamin K-dependent part of prothrombin’, FEBS Letters, 44, 189–93CrossRefGoogle Scholar
  273. Magnusson, S., Petersen, T.E., Sottrup-Jensen, L. and Claeys, H. (1975) ‘Complete primary structure of prothrombin: Isolation, structure and reactivity of ten carboxylated glutamic acid residues and regulation of prothrombin activation by thrombin’, in Proteases and Biological Control, Vol. 2, Cold Spring Harbor, pp. 123–49Google Scholar
  274. Mandle, R. and Kaplan, A.P. (1977) ‘Hageman factor substrates. Human plasma prekallikrein: mechanism of activation by Hageman factor and participation in Hageman factor-dependent fibrinolysis’, Journal of Biological Chemistry, 252, 6097–104Google Scholar
  275. Mandle, R., Colman, R.W. and Kaplan, A.P. (1976) ‘Identification of prekallikrein and HMW kininogen as circulating complex in human plasma’, Proceedings of the National Academy of Sciences, 73, 4179–83CrossRefGoogle Scholar
  276. Marciniak, E. (1970) ‘Coagulation inhibitor elicited by thrombin’, Science, 170, 452–3CrossRefGoogle Scholar
  277. Marciniak, E. (1972) ‘Inhibitor of human blood coagulation elicited by thrombin’, Journal of Laboratory and Clinical Medicine, 79, 924–34Google Scholar
  278. Marciniak, E. (1973) ‘Factor-Xa inactivation by antithrombin III: evidence for biological stabilization of factor Xa by factor V-phospholipid complex’, British Journal of Haematology, 24, 391–400CrossRefGoogle Scholar
  279. Marciniak, E. (1974) ‘Anticoagulant properties of low density lipoproteins’, Federation Proceedings, 33, 211Google Scholar
  280. Marciniak, E. and Tsukamura, S. (1972) ‘Two progressive inhibitors of factor Xa in human blood’, British Journal of Haematology, 22, 341–51CrossRefGoogle Scholar
  281. Marciniak, E., Farley, C.H. and DeSimone, P.A. (1974) ‘Familial thrombosis due to antithrombin III deficiency’, Blood, 43, 219–31Google Scholar
  282. Marder, V.J. and Shulman, N.R. (1969) ‘High molecular weight derivatives of human fibrinogen produced by plasmin. II. Mechanisms of their anticoagulant activity’, Journal of Biological Chemistry, 244, 2120–4Google Scholar
  283. Margolis, J. (1958) ‘Activation of plasma by contact with glass: evidence for a common reaction which releases plasma kinin and initiates coagulation’, Journal of Physiology, 144, 1–22Google Scholar
  284. Marlar, R.A. and Griffin, J.H. (1980) ‘Deficiency of protein C inhibitor in combined factor V/VIII deficiency disease’, Journal of Clinical Investigation, 66,1186–9CrossRefGoogle Scholar
  285. Matheson, N.R. and Travis, J. (1976) ‘Inactivation of human thrombin in the presence of human a proteinase inhibitor’, Biochemical Journal, 159, 495–502Google Scholar
  286. Matsuo, T., Ohki, Y., Kondo, S. and Matsuo, O. (1979) ‘Familial antithrombin III deficiency in a Japanese family’, Thrombosis Research, 16, 815–23CrossRefGoogle Scholar
  287. Mattock, P. and Esnouf, M.P. (1973) ‘A form of bovine factor X with a single polypeptide chain’, Nature New Biology, 242, 90–2Google Scholar
  288. McConnell, D.J. (1972) ‘Inhibitors of kallikrein in human plasma’, Journal of Clinical Investigation, 51, 1611–23CrossRefGoogle Scholar
  289. McDonagh, J., Messel, H., McDonagh, R.P., Murano, G. and Blombäck, B. (1972) ‘Molecular weight analysis of fibrinogen and fibrin chains by an improved sodium dodecyl sulphate gel electrophoresis method’, Biochimica et Biophysica Acta, 257, 135–42Google Scholar
  290. McMillin, C.R., Saito, H., Ratnoff, O.D. and Walton, A.G. (1974) ‘The secondary structure of human Hageman factor (factor XII) and its aeteration by activating agents’, Journal of Clinical Investigation, 54, 1312–22CrossRefGoogle Scholar
  291. Meier, H.L., Pierce, J.V., Colman, R.W. and Kaplan, A.P. (1977) ‘Activation and function of human Hageman factor. The role of high molecular weight kininogen and prekallikrein’, Journal of Clinical Investigation, 60, 18–31CrossRefGoogle Scholar
  292. Miletich, J.P., Jackson, CM. and Majerus, P.W. (1977) ‘Interaction of coagulation factor Xa with human platelets’, Proceedings of the National Academy of Sciences, 74, 4033–6CrossRefGoogle Scholar
  293. Miletich, J.P., Jackson, CM. and Majerus, P.W. (1978a) ‘Properties of the factor Xa binding site on human platelets’, Journal of Biological Chemistry, 253, 6908–16Google Scholar
  294. Miletich, J.P., Majerus, D.W. and Majerus, P.W. (1978b) ‘Patients with congenital factor V deficiency have decreased factor Xa binding sites on their platelets’, Journal of Clinical Investigation, 62, 824–31CrossRefGoogle Scholar
  295. Miller, L.L. and Bale, W.F. (1954) ‘Synthesis of all plasma protein fractions except gamma globulins by the liver’, Journal of Experimental Medicine, 99, 125–32CrossRefGoogle Scholar
  296. Miller, L.L., Bly, CG., Watson, M.L. and Bale, W.F. (1951) ‘Dominant role of liver in plasma protein synthesis; direct study of isolated perfused rat liver with the aid of lysine-e-C14’, Journal of Experimental Medicine, 94, 431–53CrossRefGoogle Scholar
  297. Miller-Andersson, M., Andersson, L.-O. and Borg, H. (1973) ‘Isolation and characterization of a new immediate antithrombin from human plasma’, Abstracts IVth International Congress on Thrombosis and Haemostasis, Vienna, p. 216Google Scholar
  298. Miller-Andersson, M., Borg, H. and Andersson, L.-O. (1974) ‘Purification of antithrombin III by affinity chromatography’, Thrombosis Research, 5, 439–52CrossRefGoogle Scholar
  299. Morrison-Silverberg, S.A. and Jesty, J. (1981) ‘The role of activated factor X in the control of blood coagulation’, Journal of Biological Chemistry, 256, 1625–30Google Scholar
  300. Mosesson, M.W., Escaig, J. and Feldmann, G. (1979) ‘Electron microscopy of metal-shadowed fibrinogen molecules deposited on carbon films at different concentrations’, Thrombosis and Haemostasis, 42, 88Google Scholar
  301. Moskowitz, R.W., Schwartz, H.J., Michel, B., Ratnoff, O.D. and Astrup, T. (1970) ‘Generation of kinin-like agents by chondroitin sulphate, chitin sulphate, and human articular cartilage: Possible pathophysiologic implications’, Journal of Laboratory and Clinical Medicine, 76, 790–8Google Scholar
  302. Mui, P.T.K, and Ganguly, P. (1977) ‘Cross-linking of actin and fibrin by fibrin-stabilizing factor’, American Journal of Physiology, 233, H346–9Google Scholar
  303. Murano, G., Seegers, W.H. and Zolton, R.P. (1974) ‘Autoprothrombin II-A: A competitive inhibitor of autoprothombin C (Factor Xa). A review with additions’, Thrombosis et Diathesis Haemorrhagica, Suppl. 57, 305–14Google Scholar
  304. Nachman, R.L. and Jaffe, E.A. (.1975) ‘Subcellular platelet factor VIII antigen and von Willebrand factor’, Journal of Experimental Medicine, 141, 1101–13CrossRefGoogle Scholar
  305. Nachman, R.L., Levine, R. and Jaffe, E.A. (1977) ‘Synthesis of factor-VIII antigen by cultured guinea pig megakaryocytes’, Journal of Clinical Investigation, 60, 914–21CrossRefGoogle Scholar
  306. Nakayasu, T. and Nagasawa, S. (1979) ‘Studies on human kininogens I. Isolation, characterization, and cleavage by plasma kallikrein of high molecular weight (HMW)-kininogen’, Journal of Biochemistry, 85, 249–58Google Scholar
  307. Nemerson, Y. (1968) ‘The phospholipid requirement of tissue factor in blood coagulation’, Journal of Clinical Investigation, 47, 72–80CrossRefGoogle Scholar
  308. Nemerson, Y. and Pitlick, F.A. (1970) ‘Purification and characterization of the protein component of tissue factor’, Biochemistry, 9, 5100–5CrossRefGoogle Scholar
  309. Nesheim, M.E. and Mann, K.G. (1979) ‘Thrombin-catalyzed activation of single chain bovine factor V’, Journal of Biological Chemistry, 254, 1326–34Google Scholar
  310. Nesheim, M.E., Myrmel, K.H., Hibbard, L. and Mann, K.G. (1979) ‘Isolation and characterization of single chain bovine factor V’, Journal of Biological Chemistry, 254, 508–17Google Scholar
  311. Nesheim, M.E., Kettner, C, Shaw, E. and Mann, K.G. (1981) ‘Cofactor dependence of factor Xa incorporation into the prothrombinase complex’, Journal of Biological Chemistry, 256, 6537–40Google Scholar
  312. Nesheim, M.E., Canfield, W.M., Kisiel, W. and Mann, K.G. (1982) ‘Studies of the capacity of factor Xa to protect factor Va from inactivation by activated protein C’, Journal of Biological Chemistry, 257, 1443–7Google Scholar
  313. Niewiarowski, S. and Kowalski, E. (1958) ‘Un nouvel anticoagulant derive du fibrinogene’, Revue d Hematologic, 13, 320–7Google Scholar
  314. Niewiarowski, S. and Latallo, Z. (1957) ‘Influence of plasmin on the first coagulation stage’, Bulletin de TAcademie Polonaise des Sciences, 5, 219–26Google Scholar
  315. Niewiarowski, S. and Prou-Wartelle, O. (1959) ‘Role du facteur contact (facteur Hageman) dans la fibrinolyse’, Thrombosis et Diathesis Haemorrhagica, 3, 593–606Google Scholar
  316. Nordenman, B., Nyström, C. and Björk, I. (1977) ‘The size and shape of human and bovine antithrombin IIP’, European Journal of Biochemistry, 78, 195–203CrossRefGoogle Scholar
  317. Norman, J.C., Lambilliotte, J.-P., Kojima, Y. and Sise, H.S. (1967) ‘Antihemophilic factor release by perfused liver and spleen: relationship to hemophilia’, Science, 158, 1060–1CrossRefGoogle Scholar
  318. Nossel, H.L. (1966) ‘Activation of factors XII (Hageman) and XI (PTA) by skin contact’, Proceedings of the Society for Experimental Biology and Medicine, 122, 16–7Google Scholar
  319. Nossel, H.L. and Niemetz, J. (1965) ‘A normal inhibitor of the blood coagulation contact reaction product’, Blood, 25, 712–23Google Scholar
  320. Odegard, O.R., Abildgaard, U., Lie, M. and Miller-Andersson, M. (1977) ‘Inactivation of bovine and human thrombin and factor Xa by antithrombin III studied with amidolytic methods’, Thrombosis Research, 11, 2–16CrossRefGoogle Scholar
  321. Ogston, D., Ogston, CM. and Ratnoff, O.D. (1969) ‘Studies on the clot-promoting effect of skin’, Journal of Laboratory and Clinical Medicine, 73, 70–7Google Scholar
  322. Ohishi, S., Katori, M., Han, Y.N., Iwanaga, S., Kato, H. and Suzuki, T. (1977) ‘Possible physiological role of new peptide fragments released from bovine high molecular weight kininogen by plasma kallikrein’, Biochemical Pharmacology, 26, 115–20CrossRefGoogle Scholar
  323. Olexa, S.A., Budzynski, A.Z. (1981) ‘Localisation of a fibrin polymerisation site’, Journal of Biological Chemistry, 256, 3544–9Google Scholar
  324. Olson, J.P., Miller, L.L. and Troup, S.B. (1966) ‘Synthesis of clotting factors by the isolated perfused rat liver’, Journal of Clinical Investigation, 45, 690–701CrossRefGoogle Scholar
  325. Osteoid, B. and Rapaport, S.I. (1977) ‘Activation of factor IX by the reaction product of tissue factor and factor VII: additional pathway for initiating blood coagulation’, Proceedings of the National Academy of Sciences, 74, 5260–4CrossRefGoogle Scholar
  326. Osteoid, B., Rapaport, S.I., Schiffman, S. and Chong, M.M.Y. (1971) ‘Formation of intrinsic factor X-activator activity, with special reference to the role of thrombin’, British Journal of Haematology, 21, 643–60CrossRefGoogle Scholar
  327. Osteoid, B., Berre, A., Otnaess, A.-B., Bjorklid, E. and Prydz, H. (1972) ‘Activation of the coagulation factor VII by tissue thromboplastin and calcium’, Biochemistry, 11, 2853–7CrossRefGoogle Scholar
  328. Osteoid, B., Miller-Andersson, M., Abildgaard, U. and Prydz, H. (1976) ‘The effect of antithrombin HI on the activity of the coagulation factors VII, IX and X’, Thrombosis and Haemostasis, 35, 295–304Google Scholar
  329. Osteoid, B., Rapaport, S.I. and Lavine, K.K. (1977) ‘Factor V activity of platelets: evidence for an activated factor V molecule and for a platelet activator’, Blood, 49,819–34Google Scholar
  330. Osteoid, B., Bouma, B.N. and Griffin, J.H. (1978) ‘Human blood coagulation factor IX. Purification, properties, and mechanism of activation by activated factor XI’, Journal of Biological Chemistry, 253, 5946–51Google Scholar
  331. Osterud, B., Harper, E., Rapaport, S.I. and Lavine, K. (1979) ‘Evidence against collagen activation of platelet associated factor XI as a mechanism for initiating intrinsic clotting’, Scandinavian Journal of Haematology, 22, 205–13CrossRefGoogle Scholar
  332. Otis, P.T. and Rapaport, S.I. (1973) ‘Failure of fibrinogen degradation products to increase plasma fibrinogen in rabbits’, Proceedings of the Society for Experimental Biology and Medicine, 144, 124–9Google Scholar
  333. Owen, C.A. and Bowie, E.J.W. (1977) ‘Generation of coagulation factors V, XI, and XII by the isolated rat liver’, Haemostasis, 6, 205–12Google Scholar
  334. Owen, C.A. and Bowie, E.J.W. (1981) ‘Generation of plasmatic coagulation factors by the isolated rat liver perfused with completely synthetic blood substitute’, Thrombosis Research, 22, 259–66CrossRefGoogle Scholar
  335. Owen, W.G. and Esmon, C.T. (1981) ‘Functional properties of an endothelial cell cofactor for thrombin-catalyzed activation of protein C’, Journal of Biological Chemistry, 256, 5532–5Google Scholar
  336. Owen, W.G., Esmon, C.T. and Jackson, CM. (1974) ‘The conversion of prothrombin to thrombin I. Characterization of the reaction products formed during the activation of bovine prothrombin’, Journal of Biological Chemistry, 249, 594–605Google Scholar
  337. Pearson, J.D. and Gordon, J.L. (1979) ‘Vascular endothelial and smooth muscle cells in culture selectively release adenine nucleotides’, Nature, 281, 384–6CrossRefGoogle Scholar
  338. Pepper, D.S., Gaffney, P.J. and Blume, H.D. (1974) ‘The distribution of carbohydrate in the plasmin resistant core fragments (D, E) of human fibrinogen’, Biochimica et Biophysica Acta, 365, 203–7Google Scholar
  339. Petersen, T.E., Dudek-Wojciechowska, G., Sottrup-Jensen, L. and Magnusson, S. (1979) ‘Primary structure of antithrombin III (heparin cofactor)’. Partial homology between a antitrypsin and antithrombin IIP, in D. Collen, B. Wiman and M. Verstraete (eds.) The Physiological Inhibitors of Blood Coagulation, Elsevier/North-Holland, Biomedical Press, pp. 43–54Google Scholar
  340. Petersen, T.E., Thogersen, H.C, Sottrup-Jensen, L., Magnusson, S. and Jörnvall, H. (1980) ‘Isolation and Af-terminal amino acid sequence of protein Z, a y-carboxyglutamic acid containing protein from bovine plasma’, FEBS Letters, 114, 278–82CrossRefGoogle Scholar
  341. Philip, G., Moran, J. and Colman, R.W. (1970) ‘Dissociation and association of the oligomeric forms of factor V’, Biochemistry, 9, 2212–8CrossRefGoogle Scholar
  342. Pickart, L.R. and Pilgeram, L.O. (1967) ‘The role of thrombin in fibrinogen biosynthesis’’, Thrombosis et Diathesis Haemorrhagica, 17, 358–64Google Scholar
  343. Pickart, L.R. and Thaler, M.M. (1976) ‘Free fatty acids and albumin as mediators of thrombin-stimulated fibrinogen synthesis’, American Journal of Physiology, 230, 996–1002Google Scholar
  344. Piepkorn, M.W., Lagunoff, D. and Schmer, G. (1978) ‘Heparin binding to antithrombin III: variation in binding sites and affinity’, Biochemical and Biophysical Research Communications, 85, 851–6CrossRefGoogle Scholar
  345. Pifer, D.D., Colman, R.W. and Chesney, CM. (1977) ‘Subcellular localization and secretion of factor V by human platelets’, Thrombosis and Haemostasis, 38, 126Google Scholar
  346. Pisano, J.J., Finlayson, J.S., Peyton, M.P. and Nagai, Y. (1971) ‘e (y-glutamyl) lysine in fibrin: lack of crosslink formation in factor XIII deficiency’, Proceedings of the National Academy of Sciences, 68, 770–2CrossRefGoogle Scholar
  347. Pool, J.G. and Robinson, J. (1959) ‘In vitro synthesis of coagulation factors by rat liver slices’, American Journal of Physiology, 196, 423–8Google Scholar
  348. Pouit, L., Marcille, G., Suscillon, M. and Hollard, D. (1972) ‘Etude en microscopie electronique de differentes etapes de la fibrinoformation’, Thrombosis et Diathesis Haemorrhagica, 27, 559–72Google Scholar
  349. Proud, D., Pierce, J.V. and Pisano, J.J. (1980) ‘Radioimmunoassay of human high molecular weight kininogen in normal and deficient plasmas’, Journal of Laboratory and Clinical Medicine, 95, 563–74Google Scholar
  350. Prowse, C.V., Mattock, P., Esnouf, M.P. and Russell, A.M. (1976) ‘A variant of prothrombin induced in cattle by prolonged administration of warfarin’, Biochimica et Biophysica Acta, 434, 265–79Google Scholar
  351. Radcliffe, R.D. and Barton, P.G. (1973) ‘Comparisons of the molecular forms of activated bovine factor X. Products of activation with Russell’s viper venom, insoluble trypsin, sodium citrate, tissue factor, and the intrinsic system’, Journal of Biological Chemistry, 248, 6788–95Google Scholar
  352. Radcliffe, R. and Nemerson, Y. (1975) ‘Activation and characterization of a single chain form of factor VIP’, Journal of Biological Chemistry, 250, 388–95Google Scholar
  353. Radcliffe, R. and Nemerson, Y. (1976) ‘Mechanism of activation of bovine factor VII. Products of cleavage by factor Xa’, Journal of Biological Chemistry, 251, 4797–802Google Scholar
  354. Radcliffe, R., Bagdasarian, A., Colman, R. and Nemerson, Y. (1977) ‘Activation of bovine factor VII by Hageman factor fragments’, Blood, 50, 611–7Google Scholar
  355. Ratnoff, O.D. (1968) ‘Activation of Hageman factor by L-homocystine’, Science, 162, 1007–9CrossRefGoogle Scholar
  356. Ratnoff, O.D. and Colopy, J.E. (1955) ‘A familial hemorrhagic trait associated with a deficiency of a clot-promoting fraction of plasma’, Journal of Clinical Investigation, 34, 602–13CrossRefGoogle Scholar
  357. Ratnoff, O.D. and Crum, J.D. (1964) ‘Activation of Hageman factor by solutions of ellagic acid’, Journal of Laboatory and Clinical Medicine, 63, 359–77Google Scholar
  358. Ratnoff, O.D. and Rosenblum, J.M. (1958) ‘Role of Hageman factor in the initiation of clotting by glass: evidence that glass frees Hageman factor from inhibition’, American Journal of Medicine, 25, 160–8CrossRefGoogle Scholar
  359. Ratnoff, O.D. and Saito, H. (1979a) ‘Interactions among Hageman factor, plasma kallikrein, high molecular weight kininogen, and plasma thromboplastin antecedent’, Proceedings of the National Academy of Sciences, 76, 958–61CrossRefGoogle Scholar
  360. Ratnoff, O.D. and Saito, H. (1979b) ‘Amidolytic properties of single-chain activated Hageman factor’, Proceedings of the National Academy of Sciences, 76, 1461–3CrossRefGoogle Scholar
  361. Ratnoff, O.D., Pensky, J., Ogston, D. and Naff, G.B. (1969) ‘The inhibition of plasmin, plasma kallikrein, plasma permeability factor and the Clr subcomponent of complement by serum C’l esterase inhibitor’, Journal of Experimental Medicine, 129, 315–31CrossRefGoogle Scholar
  362. Ratnoff, O.D., Pensky, J., Donaldson, V.H. and Amir, J. (1972) ‘The inhibitory properties of plasma against activated plasma thromboplastin antecedent (factor Xla) in hereditary angioneurotic edema’, Journal of Laboratory and Clinical Medicine, 80, 803–9Google Scholar
  363. Regoeczi, E. (1970) ‘Fibrinogen catabolism: kinetics of catabolism following sudden elevation of the pool with exogenous fibrinogen’, Clinical Science, 38, 111–21Google Scholar
  364. Revak, S.D. and Cochrane, CG. (1976) ‘The relationship of structure and function in human Hageman factor. The association of enzymatic and binding activities with separate regions of the molecule’, Journal of Clinical Investigation, 57, 852–60CrossRefGoogle Scholar
  365. Revak, S.D., Cochrane, CG., Johnston, A.R. and Hugh, T.E. (1974) ‘Structural changes accompanying enzymatic activation of human Hageman factor’, Journal of Clinical Investigation, 54, 619–27CrossRefGoogle Scholar
  366. Revak, S.D., Cochrane, CG. and Griffin, J.H. (1977) ‘The binding and cleavage characteristics of human Hageman factor during contact activation. Comparison of normal plasma with plasma deficient in factor XI, prekallikrein, or high molecular weight kininogen’, Journal of Clinical Investigation, 59, 1167–75CrossRefGoogle Scholar
  367. Revak, S.D., Cochrane, C.G., Bouma, B.N. and Griffin, J.H. (1978) ‘Surface and fluid phase activities of two forms of activated Hageman factor produced during contact activation of plasma’, Journal of Experimental Medicine, 147, 719–29CrossRefGoogle Scholar
  368. Rider, D.M., McDonagh, R.P. and McDonagh, J. (1978) ‘A possible contributory role of the platelet in the formation of plasma factor XIII’, British Journal of Haematology, 39, 579–88CrossRefGoogle Scholar
  369. Rimon, A., Shamash, Y. and Shapiro, B. (1966) ‘The plasmin inhibitor of human plasma, IV. Its action on plasmin, trypsin, chymotrypsin and thrombin’, Journal of Biological Chemistry, 241, 5102–7Google Scholar
  370. Rinderknecht, H. and Geokas, M.C. (1973) ‘On the physiological role of a2-macroglobulin’, Biochimica et Biophysica Acta, 295, 233–44Google Scholar
  371. Rosenberg, R.D. and Damus, P.S. (1973) ‘The purification and mechanism of action of human antithrombin-heparin cofactor’, Journal of Biological Chemistry, 248, 6490–505Google Scholar
  372. Rosenberg, R.D. and Lam, L. (1979) ‘Correlation betwee structure and function of heparin’, Proceedings of the National Academy of Sciences, 76, 1218–22CrossRefGoogle Scholar
  373. Rosenberg, J.S., McKenna, P. and Rosenberg, R.D. (1975) ‘Inhibition of human factor IXa by human antithrombin-heparin cofactor’, Journal of Biological Chemistry, 250, 8883–8Google Scholar
  374. Rosing, J., Tans, G., Covers-Riemslag, J.W.P., Zwaal, R.F.A. and Hemker, H.C. (1980) ‘The role of phospholipids and factor Va in the prothrombinase complex’, Journal of Biological Chemistry, 255, 274–83Google Scholar
  375. Ruggeri, Z.M. and Zimmerman, T.S. (1980) ‘Variant von Willebrand’s disease: Characterization of two subtypes by analysis of multimeric composition of factor VIII/von Willebrand factor in plasma and platelets’, Journal of Clinical Investigation, 65, 1318–25CrossRefGoogle Scholar
  376. Rupp, R.G. and Fuller, G.M. (1979) ‘The effects of leukocytic and serum factors on fibrinogen biosynthesis in cultured hepatocytes’, Experimental Cell Research, 118, 23–30CrossRefGoogle Scholar
  377. Saito, H. (1977) ‘Purification of high molecular weight kininogen and the role of this agent in blood coagulation’, Journal of Clinical Investigation, 60, 584–94CrossRefGoogle Scholar
  378. Saito, H. and Goldsmith, G.H. (1977) ‘Plasma thromboplastin antecedent (PTA, factor XI): a specific and sensitive radioimmunoassay’, Blood, 50, 377–85Google Scholar
  379. Saito, H., Ratnoff, O.D., Donaldson, V.H., Haney, G. and Pensky, J. (1974) ‘Inhibition of the adsorption of Hageman factor (Factor XII) to glass by normal human plasma’, Journal of Laboratory and Clinical Medicine, 84, 62–73Google Scholar
  380. Saito, H., Ratnoff, O.D., Waldmann, R. and Abraham, J.P. (1975) ‘Fitzgerald trait. Deficiency of a hitherto unrecognized agent, Fitzgerald factor, participating in surface-mediated reaction of clotting, fibrinolysis, generation of kinins, and the property of diluted plasma enhancing vascular permeability (PF/Dil)’, Journal of Clinical Investigation, 55, 1082–9CrossRefGoogle Scholar
  381. Saito, H., Ratnoff, O.D. and Pensky, J. (1976) ‘Radio-immunoassay of human Hageman factor (factor XII)’, Journal of Laboratory and Clinical Medicine, 88, 506–14Google Scholar
  382. Saito, H., Poon, M.G., Vicic, W., Goldsmith, G.H. and Menitove, J.E. (1978) ‘Human plasma prekallikrein (Fletcher factor) clotting activity and antigen in health and disease’, Journal of Laboratory and Clinical Medicine, 92, 84–94Google Scholar
  383. Saito, H., Goldsmith, G.H., Moroi, M. and Aoki, N. (1979) ‘Inhibitory spectrum of a2-plasmin inhibitor’, Proceedings of the National Academy of Sciences, 76, 2013–7CrossRefGoogle Scholar
  384. Sakariassen, K.S., Bolhuis, P.A. and Sixma, J.J. (1979) ‘Human blood platelet adhesion to artery subendothelium is mediated by factor VIII-von Willebrand factor bound to the subendothelium’, Nature, 279, 638–8CrossRefGoogle Scholar
  385. Saraswathi, S., Rawala, R. and Colman, R.E. (1978) ‘Subunit structure of bovine factor V. Influence of proteolysis during blood collection’, Journal of Biological Chemistry, 253, 1024–9Google Scholar
  386. Schapira, M., Scott, C.F. and Colman, R.W. (1981a) ‘Relative importance of plasma protease inhibitors in the inactivation of kallikrein in human plasma’, Thrombosis and Haemostasis, 46, 259Google Scholar
  387. Schapira, M., Scott, C.F. and Colman, R.W. (1981b) ‘Protection of human plasma kallikrein from inactivation by CI inhibitor and other protease inhibitors. The role of high molecular weight kininogen’, Biochemistry, 20, 2738–43CrossRefGoogle Scholar
  388. Schapira, M., Scott, C.F., James, A., Silver, L.D., Kueppers, F., James, H.L. and Colman, R.W. (1982) ‘High molecular weight kininogen or its light chain protects human plasma kallikrein from inactivation by plasma protease inhibitors’, Biochemistry, 21, 567–72CrossRefGoogle Scholar
  389. Schiffman, S. and Lee, P. (1974) ‘Preparation, characterization, and activation of a highly purified factor XI: evidence that a hitherto unrecognized plasma activity participates in the interaction of factors XI and XII’, British Journal of aematology, 27, 101–14CrossRefGoogle Scholar
  390. Schmaier, A.H., Kuchibhotla, J. and Colman, R.W. (1981) ‘High molecular weight kininogen — a secreted platelet coagulant protein’, Thrombosis and Haemostasis, 46, 96Google Scholar
  391. Schreiber, A.D., Kaplan, A.P. and Austen, K.F. (1973) ‘Inhibition by CI INA of Hageman factor fragment activation of coagulation, fibrinolysis and kinin generation’, Journal of Clinical Investigation, 52, 1402–9CrossRefGoogle Scholar
  392. Schwartz, M.L., Pizzo, S.V., Hill, R.L. and McKee, P.A. (1973) ‘Human factor XIII from plasma and platelets. Molecular weights, subunit structures, proteolytic activation, and cross-linking of fibrinogen and fibrin’, Journal of Biological Chemistry, 248, 1395–407Google Scholar
  393. Scott, C.F. and Colman, R.W. (1980) ‘Function and immunochemistry of prekallikrein-high molecular weight kininogen complex in plasma’, Journal of Clinical In vestigation, 65, 413–21CrossRefGoogle Scholar
  394. Scott, C.F., Schapira, M. and Colman, R.W. (1982a) ‘Effect of heparin on the inactivation rate of human factor Xla by antithrombin IIP’, Blood, 60, 940–7Google Scholar
  395. Scott, C.F., Schapira, M., James H.L., Cohen, A.B. and Colman, R.W. (1982b) ‘The inactivation of factor Xla by plasma protease inhibitors. Predominant role of alpha protease inhibitor and protective effect of high molecular weight kininogen’, Journal of Clinical Investigation, 69, 844–52CrossRefGoogle Scholar
  396. Scully, M.F., Ellis, V., MacGregor, I.R. and Kakkar, V.V. (1981) ‘Inhibition of human factor Xa by various plasma protease inhibitors’, Thrombosis and Haemostasis, 46, 90Google Scholar
  397. Seegers, W.H., Johnson, J.F. and Fell, C. (1954) ‘Antithrombin reaction related to prothrombin activation’, American Journal of Physiology, 176, 97–103Google Scholar
  398. Seegers, W.H., Novoa, H.E. and Henry, R. (1976) ‘Relationship of “new” vitamin K-dependent protein C and “old” autoprothrombin IIa’, Thrombosis Research, 8, 543–53CrossRefGoogle Scholar
  399. Seligsohn, U. and Klein, B. (1975) ‘The effect of leucocyte extract on fibrinogen synthesis in rabbits’, Thrombosis Research, 7, 17–24CrossRefGoogle Scholar
  400. Seligsohn, U., Rapaport, S.I. and Kuefler, P.R. (1973) ‘Extra-adrenal effect of ACTH on fibrinogen synthesis’, American Journal of Physiology, 224, 1112–1119Google Scholar
  401. Seligsohn, U., Osteoid, B., Brown, S.F., Griffin, J.H. and Rapaport, S.I. (1979) ‘Activation of human factor VII in plasma and in purified systems. Roles of activated factor IX, kallikrein, and activated factor XII’, Journal of Clinical Investigation, 64, 1056–65CrossRefGoogle Scholar
  402. Shamash, Y. and Rimon, A. (1966) ‘The plasmin inhibitors of human plasma. III. Purification and partial characterization’, Biochimica et Biophysica Acta, 121, 35–41CrossRefGoogle Scholar
  403. Shapiro, G.A., Andersen, J.C, Pizzo, S.V. and McKee, P.A. (1973) ‘The subunit structure of normal and hemophilic factor VHP’, Journal of Clinical Investigation, 52, 2198–210Google Scholar
  404. Shapiro, S.S. and Anderson, D.B. (1977) ‘Thrombin inhibition in normal plasma’, in R.L. Lundblad (ed.) Chemistry and Biology of Thrombin, Ann Arbor Science, Michigan, pp. 361–74Google Scholar
  405. Shaw, E., Giddings, J.C, Peake, I.R. and Bloom, A.L. (1979) ‘Synthesis of procoagulant factor VIII, factor VIII related antigen and other coagulation factors by the isolated perfused rat liver’, British Journal of Haematology, 41, 585–96CrossRefGoogle Scholar
  406. Silverberg, M., Dunn, J.T., Garen, L. and Kaplan, A.P. (1980) ‘Autoactivation of human Hageman factor’, Journal of Biological Chemistry, 255, 7281–6Google Scholar
  407. Smith, G.F. (1977) ‘The heparin-thrombin complex in the mechanism of thrombin inactivation by heparin’, Biochemical and Biophysical Research Communications, 77, 111–7CrossRefGoogle Scholar
  408. Smith, G.F. and Craft, T.J. (1976) ‘Heparin reacts stoichiometrically with thrombin during thrombin inhibition in human plasma’, Biochemical and Biophysical Research Communications, 71, 738–45CrossRefGoogle Scholar
  409. Smith, G.F. and Sundboom, J.L. (1981a) ‘Heparin and protease inhibition. I. Heparin complexes with thrombin, plasmin, and trypsin’, Thrombosis Research, 22, 103–14CrossRefGoogle Scholar
  410. Smith, G.F. and Sundboom, J.L. (1981b) ‘Heparin and protease inhibition. II. The role of heparin in the AT III inactivation of thrombin, plasmin and trypsin’, Thrombosis Research, 22, 115–33CrossRefGoogle Scholar
  411. Sodetz, J.M., Pizzo, S.V. and McKee, P.A. (1977) ‘Relationship of sialic acid to function and in vivo survival of human factor VIH/von Willebrand factor protein’, Journal of Biological Chemistry, 252, 5538–46Google Scholar
  412. Sodetz, J.M., Paulson, J.C, Pizzo, S.V. and McKee, P.A. (1978) ‘Carbohydrate on human factor VIII/von Willebrand factor. Impairment of function by removal of specific galactose residues’, Journal of Biological Chemistry, 253, 7202–6Google Scholar
  413. Sottrup-Jensen, L., Hansen, H.F., Mortensen, S.B., Petersen, T.E., Magnusson, S. and Jörn vail, H. (1981) ‘Mechanism of proteinase-binding to a2-macroglobulin’, Thrombosis and Haemostasis, 46, 87Google Scholar
  414. Stead, N., Kaplan, A.P. and Rosenberg, R.D. (1976) ‘Inhibition of activated factor XII by antithrombin-heparin cofactor’, Journal of Biological Chemistry, 251, 6481–8Google Scholar
  415. Steinbuch, M., Blatrix, C and Josso, F. (1967) ‘a2-macroglobulin as progressive antithrombin’, Nature, 216, 500–1CrossRefGoogle Scholar
  416. Stenflo, J. (1970) ‘Dicoumarol-induced prothrombin in bovine plasma’, Acta Chemica Scandinavica, 24, 3762–3CrossRefGoogle Scholar
  417. Stenflo, J. (1976) ‘A new vitamin K-dependent protein. Purification from bovine plasma and preliminary characterization’, Journal of Biological Chemistry, 251, 355–63Google Scholar
  418. Stenflo, J., Fernlund, P., Egan, W. and Roepstorff, P. (1974) ‘Vitamin K dependent modifications of glutamic acid residues in prothrombin’, Proceedings of the National Academy of Sciences, 71, 2730–3CrossRefGoogle Scholar
  419. Strong, D.D., Watt, K.W.K., Cottrell, B.A. and Doolittle, R.F. (1979) ‘Amino acid sequence studies on the a chain of human fibrinogen. Complete sequence of the largest cyanogen bromide fragment’, Biochemistry, 18, 5399–404CrossRefGoogle Scholar
  420. Sugo, T., Ikari, N., Kato, H., Iwanaga, S. and Fujii, S. (1980) ‘Functional sites of bovine high molecular weight kininogen as a cofactor in kaolin-mediated activation of factor XII (Hageman factor)’, Biochemistry, 19, 3215–20CrossRefGoogle Scholar
  421. Sugo, T., Kato, H., Iwanaga, S. and Fujii, S. (1981) ‘The accelerating effect of bovine plasma HMW kininogen on the surface-mediated activation of factor XII: generation of a derivative form (active kininogen) with maximal cofactor activity by limited proteolysis’, Thrombosis Research, 24, 329–37CrossRefGoogle Scholar
  422. Suomela, H., Blombäck, M. and Blombäck, B. (1977) ‘The activation of factor X evaluated by using synthetic substrates’, Thrombosis Research, 10, 267–81CrossRefGoogle Scholar
  423. Suttie, J.W. and Jackson, CM. (1977) ‘Prothrombin structure, activation and biosynthesis’, Physiological Reviews, 57, 1–70Google Scholar
  424. Takagi, T. and Doolittle, R.F. (1974) ‘Amino acid sequence studies on factor XIII and the peptide released during its activation by thrombin’, Biochemistry, 13, 750–6CrossRefGoogle Scholar
  425. Teger-Nilsson, A.C. and Ekelund, H. (1974) ‘Fibrinogen to fibrin transformation in umbilical cord blood and purified neonatal fibrinogen’, Thrombosis Research, 5, 601–12CrossRefGoogle Scholar
  426. Tesch, R., Trolp, R. and Witt, I. (1979) ‘Electron microsopic studies on the foetal fibrin clot’, Thrombosis Research, 16, 239–43CrossRefGoogle Scholar
  427. Thompson, A.R. (1977) ‘Factor IX antigen by radioimmunoassay. Abnormal factor IX protein in patients on warfarin therapy and with hemophilia B’, Journal of Clinical Investigation, 59, 900–10CrossRefGoogle Scholar
  428. Thompson, R.E., Mandle, R. and Kaplan, A.P. (1978) ‘Characterization of human high molecular weight kininogen’, Journal of Experimental Medicine, 147, 488–99CrossRefGoogle Scholar
  429. Thunberg, L., Bäckström, G., Grundberg, H., Riesenfeld, J. and Lindahl, U. (1980) ‘The molecular size of the antithrombin-binding sequence in heparin’, FEBS Letters, 7/7,203–6CrossRefGoogle Scholar
  430. Titani, K., Fujikawa, K., Enfield, D.L., Ericsson, L.H., Walsh, K.A. and Neurath, H. (1975) ‘Bovine factor XI (Stuart factor): amino-acid sequence of heavy chain’, Proceedings of the National Academy of Sciences, 72, 3082–6CrossRefGoogle Scholar
  431. Tracy, P.B., Peterson, J.M., Nesheim, M.E., McDuffie, F.C and Mann, K.G. ‘Interaction of coagulation factor V and factor Va with platelets’, Journal of Biological Chemistry, 254, 10354–61Google Scholar
  432. Tracy, P.B., Peterson, J.M., Nesheim, M.E., McDuffie, F.C. and Mann, K.G. ‘Platelet interaction with bovine coagulation factor V and factor Va’, in K.G. Mann and F.B. Taylor (eds.) The Regulation of Coagulation, Elsevier/North Holland, New York, pp. 237–43Google Scholar
  433. Tracy, P.B., Nesheim, M.E. and Mann, K.G. (1981) ‘Coordinate binding of factor Va and factor Xa to the unstimulated platelet’, Journal of Biological Chemistry, 256, 743–51Google Scholar
  434. Tracy, P.B., Eide, L.L., Bowie, E.J.W. and Mann, K.G. (1982) ‘Radioimmunoassay of factor V in human plasma and platelets’, Blood, 60, 59–63Google Scholar
  435. Triantaphyllopoulos, D.C (1958) ‘Anticoagulant effect of incubated fibrinogen’, Canadian Journal of Biochemistry and Physiology, 36, 249–59CrossRefGoogle Scholar
  436. Triantaphyllopoulos, D.C. (1959) ‘Nature of the thrombin-inhibiting effect of incubated fibrinogen’, American Journal of Physiology, 197, 575–9Google Scholar
  437. Triantaphyllopoulos, D.C. and Triantaphyllopoulos, E. (1966) ‘Evidence of antithrombic activity of the anticoagulant fraction of incubated fibrinogen’, British Journal of Physiology, 12, 145–51Google Scholar
  438. Tuszynski, G.P., Bevacqua, S.J., Schmaier, A.H., Colman, R.W. and Walsh, P.N. (1982) ‘Factor XI antigen and activity in human platelets’, Blood, 59, 1148–56Google Scholar
  439. Ulevitch, R.J., Letchford, D. and Cochrane, CG. (1974) ‘A direct enzymatic assay for the esterolytic activity of activated Hageman factor’, Thrombosis et Diathesis Haemorrhagica, 31, 30–9Google Scholar
  440. Vannucchi, S., Fibbi, G., Pasquali, F., Del Rosso, M., Cappelletti, R. and Chiarugi, V. (1982) ‘Adhesion-dependent heparin production by platelets’, Nature, 296, 352–3CrossRefGoogle Scholar
  441. Vecchione, J. and Zucker, M. (1975) ‘Procoagulant activity of platelets in recalcified plasma’, British Journal of Haematology, 31, 423–8CrossRefGoogle Scholar
  442. Vehar, G.A. and Davie, E.W. (1980) ‘Preparation and properties of bovine factor VIII (antihemophilic factor)’, Biochemistry, 19, 401–10CrossRefGoogle Scholar
  443. Venneröd, A.H., Laake, K., Solberg, A.K. and Strömland, S. (1976) ‘Inactivation and binding of human plasma kallikrein by antithrombin III and heparin’, Thrombosis Research, 9, 457–66CrossRefGoogle Scholar
  444. Vicic, W.J., Ratnoff, O.D., Saito, H. and Goldsmith, G.H. (1979) ‘Platelets and surface-mediated clotting activity’, British Journal of Haematology, 43, 91–8CrossRefGoogle Scholar
  445. Villanueva, G. and Danishefsky, I. (1979) ‘Conformational changes accompanying the binding of antithrombin III to thrombin’, Biochemistry, 18, 810–7CrossRefGoogle Scholar
  446. Walker, F.J. (1980) ‘Regulation of activated protein C by a new protein. A possible function for bovine protein S’, Journal of Biological Chemistry, 255, 5521–4Google Scholar
  447. Walker, F.J. (1981a) ‘Regulation of activated protein C by protein S’, Journal of Biological Chemistry, 256, 11128–31Google Scholar
  448. Walker, F.J. (1981b) ‘Regulation of bovine activated protein C by protein S: the role of the cofactor protein in species specificity’, Thrombosis Research, 22, 321–7CrossRefGoogle Scholar
  449. Walker, F.J., Sexton, P.W. and Esmon, C.T. (1979) ‘The inhibition of blood coagulation by activated protein C through the selective inactivation of activated factor V’, Biochimica et Biophysica Acta, 571, 333–42Google Scholar
  450. Walsh, P.N. (1972a) ‘Albumin density gradient separation and washing of platelets and the study of platelet coagulant activities’, British Journal of Haematology, 22, 205–17CrossRefGoogle Scholar
  451. Walsh, P.N. (1972b) ‘The role of platelets in the contact phase of blood coagulation’, British Journal of Haematology, 22, 237–54CrossRefGoogle Scholar
  452. Walsh, P.N. (1972c) ‘The effects of collagen and kaolin on the intrinsic coagulant activity of platelets. Evidence for an alternative pathway in intrinsic coagulation and requiring factor XII’, British Journal of Haematology, 22, 393–405CrossRefGoogle Scholar
  453. Walsh, P.N. and Griffin, J.H. (1980) ‘Contributions of human platelets to the proteolytic activation of blood coagulation factors XII and XI’, Blood, 57, 106–118Google Scholar
  454. Walz, D.A., Hewett-Emmett, D. and Seegers, W.H. (1977) ‘Amino acid sequence of human prothrombin fragments 1 and 2’, Proceedings of the National Academy of Sciences, 74, 1969–72CrossRefGoogle Scholar
  455. Ware, A.G., Fahey, J.L. and Seegers, W.H. (1948) ‘Platelet extracts, fibrin formation and interaction of purified prothrombin and thromboplastin’, American Journal of Physiology, 154, 140–7Google Scholar
  456. Wasteson, A., Glimelius, B., Busch, C, Westermark, B., Heldin, C.-H. and Norling, B. (1977) ‘Effect of a platelet endoglycosidase on cell surface associated heparan sulphate of human endothelial and glial cells’, Thrombosis Research, 11, 309–21CrossRefGoogle Scholar
  457. Watada, M, Nakagawa, M., Kitani, T., Okajima, Y., Maeda, Y., Urano, S. and Ijichi, H. (1981) ‘Identification of the AT III synthesizing hepatocytes by immunofluorescent technique’, Thrombosis and Haemostasis, 46, 284Google Scholar
  458. Watt, K.W.K., Takagi, T. and Doolittle, R.F. (1978) ‘Amino acid sequence of the ß chain of human fibrinogen: Homology with the y chain’, Proceedings of the National Academy of Sciences, 75, 1731–5CrossRefGoogle Scholar
  459. Watt, K.W.K., Cottrell, B.A., Strong, D.D. and Doolittle, R.F. (1979) ‘Amino acid sequence studies on the a chain of human fibrinogen. Overlapping sequences providing the complete sequence’, Biochemistry, 18, 5410–6CrossRefGoogle Scholar
  460. Webster, W.P., Reddick, R.L., Roberts, H.R. and Penick, G.D. (1967) ‘Release of factor VIII (anti-haemophilic factor) from perfused organs and tissues’, Nature, 213, 1146–7CrossRefGoogle Scholar
  461. Weidner, N., Ittyerah, T.R., Wochner, R.D. and Sherman, L.A. (1979) ‘Investigation of an inflammatory humoral factor as a stimulator of fibrinogen synthesis’, Thrombosis Research, 15, 651–61CrossRefGoogle Scholar
  462. Weiss, H.J. and Hoyer, L.W. (1973) ‘Von Willebrand factor: Dissociation from antihemophilic factor procoagulant activity’, Science, 182, 1149–51CrossRefGoogle Scholar
  463. Wiggins, R.C. and Cochrane, C.C. (1979) ‘The autoactivation of rabbit Hageman factor’, Journal of Experimental Medicine, 150, 1122–33CrossRefGoogle Scholar
  464. Wiggins, R.C, Bouma, B.N., Cochrane, CG. and Griffin, J.H. (1977) ‘Role of high-molecular weight kininogen in surface-binding and activation of coagulation factor XI and prekallikrein’, Proceedings of the National Academy of Sciences, 74, 4636–40CrossRefGoogle Scholar
  465. Wiggins, R.C, Loskutoff, D.J., Cochrane, CG. and Griffin, J.H. (1980) ‘Activation of rabbit Hageman factor by homogenates of cultured rabbit endothelial cells’, Journal of Clinical Investigation, 65, 197–206CrossRefGoogle Scholar
  466. Wilding, P., Adham, N.F., Mehl, J.W. and Haverback, B.J. (1967) ‘Alpha-2-macroglobulin concentrations in human serum’, Nature, 214, 1226–7CrossRefGoogle Scholar
  467. Wilner, G.D., Nossel, H.L. and Leroy, E.C (1968) ‘Activation of Hageman factor by collagen’, Journal of Clinical Investigation, 47, 2608–15CrossRefGoogle Scholar
  468. Witt, I. and Hasler, K. (1972) ‘Influence of organically bound phosphorus in foetal and adult fibrinogen on the kinetics of the interaction between thrombin and fibrinogen’, Biochimica et Biophysica Acta, 271, 357–62Google Scholar
  469. Witt, I. and Müller, H. (1970) ‘Phosphorus and hexose content of human foetal fibrinogen’, Biochimica et Biophysica Acta, 221, 402–4Google Scholar
  470. Witt, I. and Tesch, R. (1979) ‘Molecular characterization of human foetal fibrinogen’, Thrombosis and Haemostasis, 42, 79Google Scholar
  471. Witt, I., Müller, H. and Künzer, W. (1969) ‘Evidence for the existence of foetal fibrinogen’, Thrombosis et Diathesis Haemorrhagica, 22, 101–9Google Scholar
  472. Wuepper, K.D. (1972) ‘Precursor plasma thromboplastin antecedent (PTA, clotting factor XI)’, Federation Proceedings, 31, 624Google Scholar
  473. Wuepper, K.D. (1973) ‘Prekallikrein deficiency in man’, Journal of Experimental Medicine, 138, 1345–55CrossRefGoogle Scholar
  474. Wuepper, K.D. and Cochrane, CG. (1972) ‘Plasma prekallikrein: isolation, characterization, and mechanism of action’, Journal of Experimental Medicine, 135, 1–20CrossRefGoogle Scholar
  475. Wuepper, K.D., Miller, D.R. and Lacombe, M.J. (1975) ‘Flaujeac trait: deficiency of human plasma kininogen’, Journal of Clinical Investigation, 56, 1663–72CrossRefGoogle Scholar
  476. Yin, E.T., Wessler, S. and Stoll, P.J. (1971) ‘Biological properties of the naturally occurring plasma inhibitor to activated factor X’, Journal of Biological Chemistry, 246, 3703–11Google Scholar
  477. Yin, E.T., Salsgiver, W.J. and Tangen, O. (1979) ‘A hitherto undescribed naturally occurring plasma antagonist of activated factor X inhibitor (antithrombin III)’, Thrombosis and Haemostasis, 42, 122Google Scholar
  478. Young, M.C and Kolmen, S.N. (1970) ‘Recovery of fibrinogen in fibrinolytic dogs’, Thrombosis et Diathesis Haemorrhagica, 23, 50–7Google Scholar
  479. Zur, M. and Nemerson, Y. (1978) ‘The esterase activity of coagulation factor VII. Evidence for intrinsic activity of the zymogen’, Journal of Biological Chemistry, 253, 2203–9Google Scholar
  480. Zur, M. and Nemerson, Y. (1980) ‘Kinetics of factor IX activation via the extrinsic pathway. Dependence of Km on tissue factor’, Journal of Biological Chemistry, 255, 5703–7Google Scholar

Copyright information

© Derek Ogston 1983

Authors and Affiliations

  • Derek Ogston
    • 1
  1. 1.University of AberdeenUK

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