Zeitschrift für Parasitenkunde

, Volume 60, Issue 3, pp 239–247 | Cite as

The plasma cryofibrinogen of calves infected withOesophagostomum radiatum

  • B. V. Goodger
  • K. C. Bremner
Original Investigations
  • 29 Downloads

Summary

A cryofibrinogen complex was detected in the plasma of cattle infected withOesophagostomum radiatum. Its formation coincided with the development of hypofibrinogenaemia and it consisted basically of fibrinogen and soluble noncross-linked fibrin in both monomer and high molecular forms. Also present in the complex, albeit in trace amounts, were cold insoluble globulin, IgG, and plasminogen. It is suggested that the complex results from thrombin activation in vivo and its role is to maintain fibrin in solution thus preventing its deposition in the vascular system.

Keywords

Thrombin Fibrinogen Plasminogen Trace Amount Vascular System 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Bang, N.U.: Soluble fibrin complexes. Semin. Thromb. Hemostas.1, 91–128 (1974)Google Scholar
  2. Bremner, K.C., Fridemanis, R.: A defibrination syndrome in calves caused by histotrophic larvae ofOesophagostomum radiatum. J. Comp. Pathol.85, 383–390 (1975)PubMedGoogle Scholar
  3. Budzynski, A.Z., Marder, V.J.: Plasmic degradation of fibrinogen Paris 1. J. Lab. Clin. Med.88, 817–825 (1976)PubMedGoogle Scholar
  4. Chesterman, C.N.: The fibrinolytic system and haemostasis. Thromb. Haemostas.34, 368–377 (1975)Google Scholar
  5. Deykin, D.: The clinical challenge of disseminated intravascular coagulation. New Engl. J. Med.283, 636–644 (1970)PubMedGoogle Scholar
  6. Elek, P., Durie, P.H.: The histopathology of the reactions of calves to experimental infection with the nodular worm,Oesophagostomum radiatum (Rudolphi, 1803). II. Reaction of the susceptible host to infection with a single dose of larvae. Aust. J. Agric. Res.18, 549–559 (1967)Google Scholar
  7. Francis, P.B., Wilson, J.: Correlation of the serial-dilution protamine sulphate test with models of ‘hypercoagulability’ and thrombosis in dogs. Am. J. Clin. Pathol.67, 356–361 (1977)PubMedGoogle Scholar
  8. Gladner, J.A., Murtaugh, P.A., Folk, J.E., Laki, K.: Nature of peptides released by thrombin. Ann. N.Y. Acad. Sci.104, 47–52 (1963)PubMedGoogle Scholar
  9. Godal, H.C., Abildgaard, U.: Gelation of soluble fibrin in plasma by ethanol. Scand. J. Haematol.3, 342–350 (1966)PubMedGoogle Scholar
  10. Goodger, B.V.: A cold precipitable fibrinogen complex in the plasma of cattle dying from infection withBabesia argentina. Z. Parasitenkd.48, 1–7 (1975)PubMedGoogle Scholar
  11. Goodger, B.V., Wright, I.G.:Babesia bovis (argentina): observations of coagulation parameters, fibrinogen catabolism, and fibrinolysis in intact and splenectomized cattle. Z. Parasitenkd.54, 9–27 (1977)PubMedGoogle Scholar
  12. Goodger, B.V., Wright, I.G., Mahoney, D.F., McKenna, R.V.:Babesia bovis (argentina): components of the cryofibrinogen complex and their contribution to pathophysiology of infection in splenectomized calves. Z. Parasitenkd.58, 3–14 (1978)PubMedGoogle Scholar
  13. Griswold, W.R.: Selective concentration of specific antibody in serum cryoprecipitates. Int. Arch. Allergy Appl. Immunol.47, 242–248 (1974)PubMedGoogle Scholar
  14. Konttinen, Y.P., Kemppainen, L., Turunen, O.: Comparison of ethanol and protamine tests in demonstration of soluble fibrin and early products of fibrin degradation. Thromb. Haemostas.28, 342–350 (1972)Google Scholar
  15. Marder, V.J., Budzynski, A.Z.: Data for defining fibrinogen and its plasmic degradation products. Thromb. Haemostas.33, 199–207 (1975)Google Scholar
  16. Merskey, C., Lalezari, P., Johnson, A.J.: A rapid, simple, sensitive method for measuring fibrinolytic split products in human serum. Proc. Soc. Exp. Biol. Med.131, 871–875 (1969)PubMedGoogle Scholar
  17. Mosesson, M.W.: The preparation of human fibrinogen free of plasminogen. Biochim. Biophys. Acta57, 204–213 (1962)PubMedGoogle Scholar
  18. Niewiarowski, S., Gurewich, V.: Laboratory identification of intravascular coagulation. The serial dilution protamine sulfate test for the detection of fibrin monomer and fibrin degradation products. J. Lab. Clin. Med.77, 665–676 (1971)Google Scholar
  19. Rampling, M.W., Gaffney, P.J.: The sulphite precipitation method for fibrinogen measurement; its use on small samples in the presence of fibrinogen degradation products. Clin. Chim. Acta67, 43–52 (1976)PubMedGoogle Scholar
  20. Roberts, F.H.S., Elek, P., Keith, R.K.: Studies on resistance in calves to experimental infections with the nodular worm,Oesophagostomum radiatum (Rudolphi, 1803) Railliet, 1898. Aust. J. Agric. Res.13, 551–573 (1962)Google Scholar
  21. Shainoff, J.R., Page, I.H.: Significance of cryoprofibrin in fibrinogen-fibrin conversion. J. Exp. Med.116, 687–707 (1962)PubMedGoogle Scholar
  22. Sharp, A.A.: Diagnosis and management of disseminated intravascular coagulation. Br. Med. Bull.33, 265–272 (1977)PubMedGoogle Scholar
  23. Stathakis, N.E., Mosesson, M.W., Chen, A.B., Galanakis, D.K.: Cryoprecipitation of fibrin-fibrinogen complexes induced by the cold-insoluble globulin of plasma. Blood51, 1211–1222 (1978)PubMedGoogle Scholar
  24. Weber, K., Osborn, M.: The reliability of molecular weight determinations by dodecyl sulfatepolyacrylamide gel electrophoresis. J. Biol. Chem.244, 4406–4412 (1969)PubMedGoogle Scholar
  25. Wieme, R.J.: An improved technique of agar gel electrophoresis on microscope slides. Clin. Chim. Acta4, 317–321 (1959)PubMedGoogle Scholar

Copyright information

© Springer-Verlag 1979

Authors and Affiliations

  • B. V. Goodger
    • 1
  • K. C. Bremner
    • 1
  1. 1.Long Pocket LaboratoriesCSIRO, Division of Animal HealthIndooroopillyAustralia

Personalised recommendations