Thromb Haemost 1967; 18(01/02): 114-132
DOI: 10.1055/s-0038-1655022
Originalarbeiten — Original Articles — Travaux Originaux
Schattauer GmbH

Properties of Fibrinogenolysis and Fibrinolysis Products in Immune Assays

F. K Beller*
1   Department of Obstetrics and Gynecology, New York University School of Medicine
,
M Maki**
1   Department of Obstetrics and Gynecology, New York University School of Medicine
› Author Affiliations
This work was supported by a grant from the National Institute of Child Health and Human Development. HD 002 70-05.
Further Information

Publication History

Publication Date:
26 June 2018 (online)

Summary

An evaluation of split products derived from fibrinogen and fibrin gave the following results:

1. Fibrinogen can be assayed in the presence of split products by the following techniques: Fibrinogen assay according to Ratnoff and Menzie and immuno radial diffusion after heat precipitation. Using the thrombin clotting time the recovery is improved if the incubation time is extended up to 24 hrs and further by adding Ca ions.

2. On immune electrophoresis split products separate only in serum but not in plasma. If however, euglobulin fractions and acidified plasma were prepared separation occured.

3. The larger split product, fraction D, derived from fibrinogen is heat labile, whereas it is heat stabile if it is derived from fibrin. Thrombin as well as large concentrations of plasmin stabilize the split product from fibrinogen against heat.

4. The prolongation of thrombin clotting time in the presence of fibrinogenolysis split products disappears after heating. Split products derived from fibrin do not prolong the thrombin clotting time. A prolongation however, develops after heating.

5. It is suggested that differentiation between intravascular coagulation and proteolysis is possible on the basis of the combined techniques of immune electrophoresis, radial diffusion method and the thrombin clotting time before and after heating.

* Career Scientist of the Health Research Council of the City of New York, under Contract 1-127.


** WHO Senior Research Trainee. M8/181/4.

** Present Address : Dept, of Obstetrics and Gynecology Hirosaki University Hirosaki, Japan.


 
  • References

  • 1 Garner R. G, Tillet W. Biochemical studies on the fibrinolytic activity of hemolytic streptococci. J. exp. Med. 60: 255 1934;
  • 2 Ferguson J. H. Assay of tryptases by lysis of fibrinogen. Proc. Soc. exp. Biol. (N. Y) 52: 243 1943;
  • 3 Glas P, Beller F. K. Inhibition of clotting as the result of plasminogen activation by streptokinase. Thrombos. Diathes. haemorrh. (Stuttg) 04: 507 1960;
  • 4 Niewarowski S, Kowalski E. Formation of an antithrombin like anticoagulant during proteolysis of fibrinogen. Bull. Acadpol. Sei. Ser. Sc. Biol. 05: 169 1957;
  • 5 Niewarowski S, Kowalski E. Un nouvel anticoagulant derive du fibrinogene. Rev. Hémat. 13: 320 1958;
  • 6 Triantaphyllopoulos D. G. Anticoagulant effect of incubated fibrinogen. Can. J. Biochem. 36: 250 1958;
  • 7 Seligman M. Possibilité d’étude immunochimique de la fibrinolyse. Rev. franç. Etud. clin. Biol. 03: 1073 1958;
  • 8 Nussenzweig V, Seligman M. Le products de dégradation du fibrinogène. Annales Inst. Pasteur. 100: 490 1961;
  • 9 Salmon J. Etude immunochimique du fibrinogène et de ses dérivés. Clin. chim. Acta. 04: 767 1959;
  • 10 Nussenzweig V, Seligman M. Dégradation par la plasmine du fibrinogène humain. Rev. Hémat. 15: 451 1960;
  • 11 Larrieu M. J, Marder V. J, Inceman S. Effects of fibrinogen degradation products on platelets and coagulation. Diffuse intravascular clotting. Trans, of the Conf. of the Internat. Comm, on Hemostasis and Thrombosis. Schattauer, Stuttgart; 1966
  • 12 Alkjaersig N, Fletcher A. P, Sherry S. Pathogenesis of the coagulation defect developing during pathological plasma proteolytic activity (“fibrinolytic”) states. II. The significance, mechanism and consequences of defective fibrin polymerization. J. clin. Invest 41: 917 1962;
  • 13 Lewis J. H, Wilson J. H. Fibrinogen breakdown products. Amer. J. Physiology 209: 1053 1964;
  • 14 Gajewski J, Alexander B. Effect of plasmin on fibrinogen and fibrin. Amer. J. Physiol. 209: 79 1964;
  • 16 Ouchterlony O. Antigen-Antibody reactions in cells. Kemi Mineral Geol. 26B: 1 1948;
  • 17 Grabar P, Burtin P. Analyse immuno-électrophorétique. Masson & Cie; Paris: 1960
  • 18 Scheidegger J. June micro-méthode de l’immunoélectrophorése. Intern. Arch. Allergy 07: 103 1955;
  • 19 Schwick G, Störiko K. Qualitative and quantitative determination of plasma proteins by immunoprécipitation. Lab. Synopsis 01: 1 1965;
  • 20 Schwicjc G. Immunochemistry of fibrinogen. In: Fibrinogen and Fibrin, Turnover of Clotting Factors. Schattauer; Stuttgart: 1964
  • 21 Mancini S, Vaerman J. P, Carbonarct O, Heremans J. F. A single radial diffusion method for the immunological quantitation of proteins. In: Peters H. (Ed) Proc. Xlth Colloquim Protides of the Biolog. Fluids. Brugge. 1963: 370 Elzevier: Amsterdam; 1964
  • 22 Ratnoff O. D, Menzie C. A new method for the determination of fibrinogen in small samples of plasma. J. Lab. clin. Med. 37: 316 1951;
  • 23 Schulz F. H. Eine einfache Bewertungsmethode von Leberparenchymschäden (volumetrische Fibrinbestimmung. Acta hepat. (Hamburg) 03: 306 1955;
  • 24 Hedner U, Nilsson I. M. Determination of plasminogen in human plasma by a casein method. Thrombos. Diathes. haemorrh. (Stuttg) 14: 545 1965;
  • 25 Seegers W. H, Nieft M. L, Vandenbelt J. M. Decompensation products of fibrinogen and fibrin. Arch. Biochem. 07: 15 1945;
  • 26 Beller F. K, Reinhardt U. Untersuchungen über die Inaktivierung von Streptokinaseaktiviertem Plasmin. Blut. 04: 367 1958;
  • 27 Abe T, Deutsch E. Einfluß von Jonenaustauschern auf die durch Streptokinase induzierbare fibrinolytische Aktivität. Wien. Z. inn. Med. 40: 52 1959;
  • 28 Triantaphyllopoulos D. G. Nature of the thrombin-inhibiting effect of incubated fibrinogen. Amer. J. Physiol. 197: 575 1959;
  • 29 Maki M, Kikuchi I, Murakami A. Anticoagulant activity of digest products of fibrinogen by plasmin. Tohoku J. exp. Med. 84: 201 1964;
  • 30 Hirsh J. A, Fletcher P, Sherry S. Effect of fibrin and fibrinogen proteolysis products on clot physical properties. Amer. J. Physiol. 209: 415 1965;
  • 31 Bang N. U. Normal and abnormal fibrin polymerisation. Thrombos. Diathes. haemorrh. (Stuttg.) Suppl. 13: 131 1963;