Thromb Haemost 1957; 01(02): 264-288
DOI: 10.1055/s-0038-1656178
Übersichten – Reviews – Revues générales
Schattauer GmbH

Studies on the Fibrinolytic Enzyme of Human Plasma[*])

Sol Sherry
1   Medical Section, The Research Institute of the Jewish Hospital of St. Louis, and the Department of Internal Medicine, Washington University, School of Medicine, St. Louis, Mo.
,
Norma Alkjaersig
1   Medical Section, The Research Institute of the Jewish Hospital of St. Louis, and the Department of Internal Medicine, Washington University, School of Medicine, St. Louis, Mo.
› Author Affiliations
Further Information

Publication History

Publication Date:
05 June 2018 (online)

 

 


#

* Supported by grants from the National Heart Institute, National Institutes of Health, USPHS, and the Lederle Laboratories Division, American Cyanamid Co.


  • References

  • 1 Tillell W. S, and Garner R. L. The fibrinolytic activity of hemolytic streptococci. J. exp. Med. 58: 485 1933;
  • 2 Milstone H. A factor in normal human blood which participates in streptococcal fibrinolysis. J. Immunol. 42: 109 1941;
  • 3 Kaplan M. H. Nature and role of the lytic factor in hemolytic streptococcal fibrinolysis. Proc. Soc. exp. biol. (N. Y.) 57: 40 1944;
  • 4 Christensen L. R. Streptococcal fibrinolysis: A proteolytic reaction due to a serum enzyme activated by streptococcal fibrinolysin. J. gen. Physiol. 28: 363 1945;
  • 5 Macfarlane R. G, and Biggs R. Fibrinolysis. Its mechanism and significance. Blood 3: 1167 1948;
  • 6 Dastre A. Fibrinolyse dans le sang. Arch, de Physiol. Norm, et Pathol. Par. 5: 661 1893;
  • 7 Nolf P. Des modifications de la coagulation du sang chez le chien après extirpation du foie. Arch. Int. Physiol. 3: 1 1905;
  • 8 Macfarlane R. G. Blood coagulation, with particular reference to the early stages. Physiol. Rev. 36: 479 1956;
  • 9 Denys J, and Marbaix H. De. Les peptonisations provoquées par le chloroforme. Cellule 5: 197 1889;
  • 10 Delezenne C, and Pozerski E. Action du serum sanguin sur la gelatine en présence du chloroforme. C. R. Soc. Biol., (Paris) 55: 327 1903;
  • 11 Opie E. L, Barker B. I, and Dochez A. R. Changes in the proteolytic enzymes and anti-enzymes of the blood serum produced by substances (chloroform and phosphorus) which cause degenerative changes in the liver. J. exp. Med. 13: 162 1911;
  • 12 Tagnon H. J, Davidson C. S, and Taylor F. H. L. The coagulation defect in hemophilia; a comparison of the proteolytic activity of chloroform preparations of hemophilic and normal plasma. J. clin. Invest. 22: 127 1943;
  • 13 Delezenne C, and Pozerski E. Action kinasique du serum sanguin préalablement traité par le chloroforme. C. R. Soc. Biol. (Paris) 55: 693 1903;
  • 14 Grob D. The antiproteolytic activity of serum; nature and experimental variation of antiproteolytic activity of serum. J. gen. Physiol. 26: 405 423, 431 1943;
  • 15 Johnson S. A, and Schneider C. L. The existence of antifibrinolysin activity in platelets. Science 117: 229 1953;
  • 16 Christensen L. R. The activation of plasminogen by chloroform. J. gen. Physiol. 30: 149 1946;
  • 17 Christensen L. R, and MacLeod C. M. A proteolytic enzyme of serum: Characterization, activation, and reaction with inhibitors. J. gen. Physiol. 28: 559 1945;
  • 18 Troll W, Sherry S, and Wachmann J. The action of plasmin on synthetic substrates. J. biol. Chem. 208: 85 1954;
  • 19 Christensen L. R, in McCarty M. The streptokinase plasminogen system. Streptococcal Infections 1954. Columbia U. Press; N. Y.: 39.
  • 20 Sherry S. The fibrinolytic activity of streptokinase activated human plasmin. J. clin. Invest. 33: 1054 1954;
  • 21 Kline D. L. The purification and crystallization of plasminogen (Profibrinolysin). J. biol. Chem. 204: 949 1953;
  • 22 Shulman S, Alkjaersig N, and Sherry S. To be published
  • 23 Sherry S, and Alkjaersig N. Studies on the activation of human plasminogen (Abst.) J. clin. Invest. 35: 735 1956;
  • 24 Ferguson J. H, in Flynn J. E. Blood Clotting and Allied Problems, Transactions of the second conference, 1949, The Josiah Macy, Jr. Foundation, N. Y., p. 174
  • 25 Sherry S, Titehener A, Gottesman L, Wassermann and Troll W. The enzymatic dissolution of experimental arterial thrombi in the dog by trypsin, chymotrypsin, and plasminogen activators. J. clin. Invest. 33: 1303 1954;
  • 26 Pillemer L, Ratnoff O. D, Blum L, and Lepow I. H. The inactivation of complement and its components by plasmin. J. exp. Med. 97: 573 1952;
  • 27 Tillell W. S, Johnson A. J, and McCarty W. R. The intravenous infusion of the streptococcal fibrinolytic principle (streptokinase) into patients. J. clin. Invest. 34: 169 1955;
  • 28 Ratnoff O. D. Fibrinogen and fibrin as stubstrates for the proteolytic enzyme of plasma. J. Clin. Invest 32: 473 1953;
  • 29 Holmberg C. G. Cleavage of fibrin by fibrinolysin from hemolytic streptococci. Arkiv. Kemi, Minerol. et Geoi. 17 A, No. 28: 1 1944;
  • 30 Franklin A. E, Quastel J. H, and Van Straten S. F. Paper chromatography of protein mixtures and blood plasma. Proc. Soc. exp. Biol. (N. Y.) 77: 783 1951;
  • 31 Shulman S. Action of fibrinolysin on fibrinogen. Fed. Proc 14: 280 1955;
  • 32 Neurath H, and Schwert G. W. The mode of action of crystalline pancreatic proteolytic enzymes. Chem. Rev 46: 69 1950;
  • 33 Neurath H. N. Y. Academy of Sciences. Conference on Proteolytic Enzymes and their Clinical Application. To be published
  • 34 Remmert L. F, and Cohen P. Partial purification and properties of a proteolytic enzyme of human serum. J. biol. Chem. 181: 431 1949;
  • 35 Christensen L. R. Methods for measuring the components of the streptococcal fibrinolytic system, and streptococcal desoxyribonuclease. J. clin. Invest 28: 163 1949;
  • 36 Loomis E. C, Ryder A, and George Jr. C. Fibrinolysin: Nomenclature, unit, assay, preparation and properties. Arch. Biochem 12: 1 1947;
  • 37 Kaplan M. H. Studies of streptococcal fibrinolysis. I. The dissimilarity of serum protease and trypsin as indicated by the separate spezificities of their kinases, fibrinolysin and enterokinase. J. clin. Invest 25: 331 1946;
  • 38 Astrup T, and Mullertz S. The fibrin plate method for estimating fibrinolytic activity. Arch. Biochem. & Biophys. 40: 346 1952;
  • 39 Lassen M. Heat cienaturation of plasminogen in the fibrin plate method. Acta physiol. Scandinav. 27: 371 p. 152.
  • 40 Astrup T. Fibrinolysis in the organism. Blood 11: 781 1956;
  • 41 Lassen M. To be published
  • 42 Mertz E. T, and Dalby A. Purification of trypsin — activated bovine fibrinolysin. (Abstract). J. Mich. med. Soc 55: 967 1956;
  • 43 Sherry S, and Alkjaersig N. Biochemical, experimental and clinical studies with proteolytic enzymes (with particular reference to the fibrinolytic enzyme of human plasma). N. Y. Academy of Sciences on Proteolytic Enzymes and their Clinical Application. To be published
  • 44 Ploug J. and Kjeldgaard Isolation of a plasminogen activator (urokinase) from urine. Arch. Biochem. Biophys. 62: 500 1956;
  • 45 Lineweaver H, and Burk D. Determining of enzyme dissociation constants. J. Am. chem. Soc 56: 658 1934;
  • 46 Troll W, and Sherry S. The activation of human plasminogen by streptokinase. J. biol. Chem. 213: 881 1955;
  • 47 Geiger W. B. Involvement of a complement-like factor in the activation of blood protease. J. Immunol. 69: 597 1952;
  • 48 Mullertz S, and Lassen M. An activator system in blood indispensable for formation of plasmin by streptokinase. Proc. Soc. exp. Biol. (N. Y.) 82: 264 1953;
  • 49 Kline D. L. N. U. Academy of Sciences Conference on Proteolytic Enzymes and their Clinical Application. To be published
  • 50 Ablondi F. B, Hagan J. J, and Hutchings B. L. Personal communication
  • 51 Astrup T, and Permin P. M. Fibrinolysis in the animal organism. Nature (Lond.) 159: 681 1947;
  • 52 Goldhaber P, Cornman I, and Ormsbee R. A. Experimental alteration of the ability of tumor cells to lys e plasma clots in vitro. Proc. Soc. exp. Biol. (N. Y.) 66: 590 1947;
  • 53 Tagnon H. J, and Palade G. E. Activation of proplasmin by a factor from mammalian tissue. J. clin. Invest. 29: 317 1950;
  • 54 Lewis J. H, and Ferguson J. H. Studies on a proteolytic enzyme system of the blood. II. Fibrinolysokinase activators for Profibrinolysin. J. clin. Invest. 29: 1059 1950;
  • 55 Lewis J. H, and Ferguson J. H. A proteolytic enzyme system of the blood. III. Activation of dog serum Profibrinolysin by staphylokinase. Am. J. Physiol. 166: 594 1951;
  • 56 Mullertz S. A plasminogen activator in spontaneously active human blood. Proc. Soc. exp. Biol. (N. Y.) 82: 291 1953;
  • 57 Lewis J. H, and Ferguson J. H. Studies on a proteolytic enzyme system of the blood. IV. Activation of Profibrinolysin by serum fibrinolysokinase. Proc. Soc. exp. Biol. (N. Y.) 78: 184 1951;
  • 58 Loomis E. C, Ryder A, and George Jr. C. Fibrinolysin and anti-fibrinolysin: Biochemical concentration of anti-fibrinolysin. Arch. Biochem. 20: 444 1949;
  • 59 Shulman N. R. Studies on the inhibition of proteolytic enzymes by serum. I. The mechanism of the inhibition of trypsin, plasmin, and chymotrypsin by serum, using fibrin tagged with I131 as a substrate. J. exp. Med. 95: 571 1952;
  • 60 Shulman N. R. Studies on the inhibition of proteolytic enzymes by serum. II. Demonstration that separate proteolytic inhibitors exist in serum; their distinctive properties and the specificity of their action. J. exp. Med. 95: 593 1952;
  • 61 Stefanini M, and Murphy I. S. Studies on platelets XIV. Human platelets as a source of antifibrinolysin. J. clin. Invest. 35: 355 1956;
  • 62 Ungar G. Release of proteolytic enzyme in anaphylactic and peptone shock in vitro. Lancet 252: 708 1947;
  • 63 Ungar G, and Mist S. Observations on release of serum fibrinolysin by specific antigen, peptone, and certain polysaccharides. J. exp. Med. 90: 39 1949;
  • 64 Rochae Silva M, and Teixeira R. M. Role played by leucocytes, platelets and plasma trypsin in peptone shock in dog. Proc. Soc. exp. Biol. (N. Y.) 61: 376 1946;
  • 65 Tillett W. S. Studies on the enzymatic lysis of fibrin and inflammatory exudates by products of hemolytic streptococci. Harvey Lectures, 1949-50, p. 149
  • 66 Tillett W. S, Johnson A. J, and McCarty W. R. Studies on the intravenous infusion of the streptococcal fibrinolytic principle (streptokinase) into patients. J. clin. Invest. 34: 169 1955;
  • 67 Ratnoff O. D. Studies on proteolytic enzyme in human plasma. IV. The rate of lysis of plasma clots in normal and diseased individuals with particular reference to hepatic disease. Bull. Johns Hopk. Hosp. 83: 29 1949;
  • 68 Tagnon H. J, Levenson S. M, Davidson C. S, and Taylor F. H. L. The occurence of fibrinolysis in shock, with observations on the prothrombin time and the plasma fibrinogen during hemorrhagic shock. Am. J. med. Sci. 211: 88 1946;
  • 69 Colgan J, Gates E, and Miller L. L. Serum and urinary fibrinolytic activity related to the hemorrhagic diathesis in irradiated dogs. J. exp. Med. 95: 531 1952;
  • 70 Fantl P, and Simon S. E. Fibrinolysis following electrically induced convulsions. J. Exper. Biol. & M. Soc 26: 521 1948;
  • 71 Latner A. L. Anxiety as a cause of fibrinolysis. Lancet 1: 194 1947;
  • 72 Biggs Macfarlane R. G, and Pilling J. Observations on fibrinolysis. Experimental activity produced by exercise or adrenalin. Lancet 1: 402 1947;
  • 73 Albrechtsen O. K, Storm O, and Trolle D. Fibrinolytic activity in the circulating blood following amniotic fluid infusion. Acta haemat. (Basel) 14: 309 1955;
  • 74 Tagnon H. J, Whitmore W. F, and Shulman N. R. Fibrinolysin in metastatic cancer of the prostate. Cancer (N. Y.) 5: 9 1952;
  • 75 Sherry S, Callaway D. W, and Freiberg R. Prevention of postoperative adhesions in the dog by intravenous injections of plasminogen activators. Proc. Soc. exp. Biol. (N.Y.) 90: 1 1955;

  • References

  • 1 Tillell W. S, and Garner R. L. The fibrinolytic activity of hemolytic streptococci. J. exp. Med. 58: 485 1933;
  • 2 Milstone H. A factor in normal human blood which participates in streptococcal fibrinolysis. J. Immunol. 42: 109 1941;
  • 3 Kaplan M. H. Nature and role of the lytic factor in hemolytic streptococcal fibrinolysis. Proc. Soc. exp. biol. (N. Y.) 57: 40 1944;
  • 4 Christensen L. R. Streptococcal fibrinolysis: A proteolytic reaction due to a serum enzyme activated by streptococcal fibrinolysin. J. gen. Physiol. 28: 363 1945;
  • 5 Macfarlane R. G, and Biggs R. Fibrinolysis. Its mechanism and significance. Blood 3: 1167 1948;
  • 6 Dastre A. Fibrinolyse dans le sang. Arch, de Physiol. Norm, et Pathol. Par. 5: 661 1893;
  • 7 Nolf P. Des modifications de la coagulation du sang chez le chien après extirpation du foie. Arch. Int. Physiol. 3: 1 1905;
  • 8 Macfarlane R. G. Blood coagulation, with particular reference to the early stages. Physiol. Rev. 36: 479 1956;
  • 9 Denys J, and Marbaix H. De. Les peptonisations provoquées par le chloroforme. Cellule 5: 197 1889;
  • 10 Delezenne C, and Pozerski E. Action du serum sanguin sur la gelatine en présence du chloroforme. C. R. Soc. Biol., (Paris) 55: 327 1903;
  • 11 Opie E. L, Barker B. I, and Dochez A. R. Changes in the proteolytic enzymes and anti-enzymes of the blood serum produced by substances (chloroform and phosphorus) which cause degenerative changes in the liver. J. exp. Med. 13: 162 1911;
  • 12 Tagnon H. J, Davidson C. S, and Taylor F. H. L. The coagulation defect in hemophilia; a comparison of the proteolytic activity of chloroform preparations of hemophilic and normal plasma. J. clin. Invest. 22: 127 1943;
  • 13 Delezenne C, and Pozerski E. Action kinasique du serum sanguin préalablement traité par le chloroforme. C. R. Soc. Biol. (Paris) 55: 693 1903;
  • 14 Grob D. The antiproteolytic activity of serum; nature and experimental variation of antiproteolytic activity of serum. J. gen. Physiol. 26: 405 423, 431 1943;
  • 15 Johnson S. A, and Schneider C. L. The existence of antifibrinolysin activity in platelets. Science 117: 229 1953;
  • 16 Christensen L. R. The activation of plasminogen by chloroform. J. gen. Physiol. 30: 149 1946;
  • 17 Christensen L. R, and MacLeod C. M. A proteolytic enzyme of serum: Characterization, activation, and reaction with inhibitors. J. gen. Physiol. 28: 559 1945;
  • 18 Troll W, Sherry S, and Wachmann J. The action of plasmin on synthetic substrates. J. biol. Chem. 208: 85 1954;
  • 19 Christensen L. R, in McCarty M. The streptokinase plasminogen system. Streptococcal Infections 1954. Columbia U. Press; N. Y.: 39.
  • 20 Sherry S. The fibrinolytic activity of streptokinase activated human plasmin. J. clin. Invest. 33: 1054 1954;
  • 21 Kline D. L. The purification and crystallization of plasminogen (Profibrinolysin). J. biol. Chem. 204: 949 1953;
  • 22 Shulman S, Alkjaersig N, and Sherry S. To be published
  • 23 Sherry S, and Alkjaersig N. Studies on the activation of human plasminogen (Abst.) J. clin. Invest. 35: 735 1956;
  • 24 Ferguson J. H, in Flynn J. E. Blood Clotting and Allied Problems, Transactions of the second conference, 1949, The Josiah Macy, Jr. Foundation, N. Y., p. 174
  • 25 Sherry S, Titehener A, Gottesman L, Wassermann and Troll W. The enzymatic dissolution of experimental arterial thrombi in the dog by trypsin, chymotrypsin, and plasminogen activators. J. clin. Invest. 33: 1303 1954;
  • 26 Pillemer L, Ratnoff O. D, Blum L, and Lepow I. H. The inactivation of complement and its components by plasmin. J. exp. Med. 97: 573 1952;
  • 27 Tillell W. S, Johnson A. J, and McCarty W. R. The intravenous infusion of the streptococcal fibrinolytic principle (streptokinase) into patients. J. clin. Invest. 34: 169 1955;
  • 28 Ratnoff O. D. Fibrinogen and fibrin as stubstrates for the proteolytic enzyme of plasma. J. Clin. Invest 32: 473 1953;
  • 29 Holmberg C. G. Cleavage of fibrin by fibrinolysin from hemolytic streptococci. Arkiv. Kemi, Minerol. et Geoi. 17 A, No. 28: 1 1944;
  • 30 Franklin A. E, Quastel J. H, and Van Straten S. F. Paper chromatography of protein mixtures and blood plasma. Proc. Soc. exp. Biol. (N. Y.) 77: 783 1951;
  • 31 Shulman S. Action of fibrinolysin on fibrinogen. Fed. Proc 14: 280 1955;
  • 32 Neurath H, and Schwert G. W. The mode of action of crystalline pancreatic proteolytic enzymes. Chem. Rev 46: 69 1950;
  • 33 Neurath H. N. Y. Academy of Sciences. Conference on Proteolytic Enzymes and their Clinical Application. To be published
  • 34 Remmert L. F, and Cohen P. Partial purification and properties of a proteolytic enzyme of human serum. J. biol. Chem. 181: 431 1949;
  • 35 Christensen L. R. Methods for measuring the components of the streptococcal fibrinolytic system, and streptococcal desoxyribonuclease. J. clin. Invest 28: 163 1949;
  • 36 Loomis E. C, Ryder A, and George Jr. C. Fibrinolysin: Nomenclature, unit, assay, preparation and properties. Arch. Biochem 12: 1 1947;
  • 37 Kaplan M. H. Studies of streptococcal fibrinolysis. I. The dissimilarity of serum protease and trypsin as indicated by the separate spezificities of their kinases, fibrinolysin and enterokinase. J. clin. Invest 25: 331 1946;
  • 38 Astrup T, and Mullertz S. The fibrin plate method for estimating fibrinolytic activity. Arch. Biochem. & Biophys. 40: 346 1952;
  • 39 Lassen M. Heat cienaturation of plasminogen in the fibrin plate method. Acta physiol. Scandinav. 27: 371 p. 152.
  • 40 Astrup T. Fibrinolysis in the organism. Blood 11: 781 1956;
  • 41 Lassen M. To be published
  • 42 Mertz E. T, and Dalby A. Purification of trypsin — activated bovine fibrinolysin. (Abstract). J. Mich. med. Soc 55: 967 1956;
  • 43 Sherry S, and Alkjaersig N. Biochemical, experimental and clinical studies with proteolytic enzymes (with particular reference to the fibrinolytic enzyme of human plasma). N. Y. Academy of Sciences on Proteolytic Enzymes and their Clinical Application. To be published
  • 44 Ploug J. and Kjeldgaard Isolation of a plasminogen activator (urokinase) from urine. Arch. Biochem. Biophys. 62: 500 1956;
  • 45 Lineweaver H, and Burk D. Determining of enzyme dissociation constants. J. Am. chem. Soc 56: 658 1934;
  • 46 Troll W, and Sherry S. The activation of human plasminogen by streptokinase. J. biol. Chem. 213: 881 1955;
  • 47 Geiger W. B. Involvement of a complement-like factor in the activation of blood protease. J. Immunol. 69: 597 1952;
  • 48 Mullertz S, and Lassen M. An activator system in blood indispensable for formation of plasmin by streptokinase. Proc. Soc. exp. Biol. (N. Y.) 82: 264 1953;
  • 49 Kline D. L. N. U. Academy of Sciences Conference on Proteolytic Enzymes and their Clinical Application. To be published
  • 50 Ablondi F. B, Hagan J. J, and Hutchings B. L. Personal communication
  • 51 Astrup T, and Permin P. M. Fibrinolysis in the animal organism. Nature (Lond.) 159: 681 1947;
  • 52 Goldhaber P, Cornman I, and Ormsbee R. A. Experimental alteration of the ability of tumor cells to lys e plasma clots in vitro. Proc. Soc. exp. Biol. (N. Y.) 66: 590 1947;
  • 53 Tagnon H. J, and Palade G. E. Activation of proplasmin by a factor from mammalian tissue. J. clin. Invest. 29: 317 1950;
  • 54 Lewis J. H, and Ferguson J. H. Studies on a proteolytic enzyme system of the blood. II. Fibrinolysokinase activators for Profibrinolysin. J. clin. Invest. 29: 1059 1950;
  • 55 Lewis J. H, and Ferguson J. H. A proteolytic enzyme system of the blood. III. Activation of dog serum Profibrinolysin by staphylokinase. Am. J. Physiol. 166: 594 1951;
  • 56 Mullertz S. A plasminogen activator in spontaneously active human blood. Proc. Soc. exp. Biol. (N. Y.) 82: 291 1953;
  • 57 Lewis J. H, and Ferguson J. H. Studies on a proteolytic enzyme system of the blood. IV. Activation of Profibrinolysin by serum fibrinolysokinase. Proc. Soc. exp. Biol. (N. Y.) 78: 184 1951;
  • 58 Loomis E. C, Ryder A, and George Jr. C. Fibrinolysin and anti-fibrinolysin: Biochemical concentration of anti-fibrinolysin. Arch. Biochem. 20: 444 1949;
  • 59 Shulman N. R. Studies on the inhibition of proteolytic enzymes by serum. I. The mechanism of the inhibition of trypsin, plasmin, and chymotrypsin by serum, using fibrin tagged with I131 as a substrate. J. exp. Med. 95: 571 1952;
  • 60 Shulman N. R. Studies on the inhibition of proteolytic enzymes by serum. II. Demonstration that separate proteolytic inhibitors exist in serum; their distinctive properties and the specificity of their action. J. exp. Med. 95: 593 1952;
  • 61 Stefanini M, and Murphy I. S. Studies on platelets XIV. Human platelets as a source of antifibrinolysin. J. clin. Invest. 35: 355 1956;
  • 62 Ungar G. Release of proteolytic enzyme in anaphylactic and peptone shock in vitro. Lancet 252: 708 1947;
  • 63 Ungar G, and Mist S. Observations on release of serum fibrinolysin by specific antigen, peptone, and certain polysaccharides. J. exp. Med. 90: 39 1949;
  • 64 Rochae Silva M, and Teixeira R. M. Role played by leucocytes, platelets and plasma trypsin in peptone shock in dog. Proc. Soc. exp. Biol. (N. Y.) 61: 376 1946;
  • 65 Tillett W. S. Studies on the enzymatic lysis of fibrin and inflammatory exudates by products of hemolytic streptococci. Harvey Lectures, 1949-50, p. 149
  • 66 Tillett W. S, Johnson A. J, and McCarty W. R. Studies on the intravenous infusion of the streptococcal fibrinolytic principle (streptokinase) into patients. J. clin. Invest. 34: 169 1955;
  • 67 Ratnoff O. D. Studies on proteolytic enzyme in human plasma. IV. The rate of lysis of plasma clots in normal and diseased individuals with particular reference to hepatic disease. Bull. Johns Hopk. Hosp. 83: 29 1949;
  • 68 Tagnon H. J, Levenson S. M, Davidson C. S, and Taylor F. H. L. The occurence of fibrinolysis in shock, with observations on the prothrombin time and the plasma fibrinogen during hemorrhagic shock. Am. J. med. Sci. 211: 88 1946;
  • 69 Colgan J, Gates E, and Miller L. L. Serum and urinary fibrinolytic activity related to the hemorrhagic diathesis in irradiated dogs. J. exp. Med. 95: 531 1952;
  • 70 Fantl P, and Simon S. E. Fibrinolysis following electrically induced convulsions. J. Exper. Biol. & M. Soc 26: 521 1948;
  • 71 Latner A. L. Anxiety as a cause of fibrinolysis. Lancet 1: 194 1947;
  • 72 Biggs Macfarlane R. G, and Pilling J. Observations on fibrinolysis. Experimental activity produced by exercise or adrenalin. Lancet 1: 402 1947;
  • 73 Albrechtsen O. K, Storm O, and Trolle D. Fibrinolytic activity in the circulating blood following amniotic fluid infusion. Acta haemat. (Basel) 14: 309 1955;
  • 74 Tagnon H. J, Whitmore W. F, and Shulman N. R. Fibrinolysin in metastatic cancer of the prostate. Cancer (N. Y.) 5: 9 1952;
  • 75 Sherry S, Callaway D. W, and Freiberg R. Prevention of postoperative adhesions in the dog by intravenous injections of plasminogen activators. Proc. Soc. exp. Biol. (N.Y.) 90: 1 1955;