Thromb Haemost 1965; 13(01): 187-193
DOI: 10.1055/s-0038-1656224
Originalarbeiten — Original Articles — Travaux Originaux
Schattauer GmbH Schattauer

Addition of Prothrombin to Blood from Dogs Receiving Dicumarol[*]

Heinz Schröer
1   Department of Physiology and Pharmacology, Wayne State University, School of Medicine, Detroit, Michigan, U.S.A.
,
D. L Heene
1   Department of Physiology and Pharmacology, Wayne State University, School of Medicine, Detroit, Michigan, U.S.A.
,
W. H Seegers
1   Department of Physiology and Pharmacology, Wayne State University, School of Medicine, Detroit, Michigan, U.S.A.
› Author Affiliations
Further Information

Publication History

Publication Date:
24 July 2018 (online)

Summary

The prothrombin concentration of dog plasma was lowered by giving large doses of Dicumarol. The dog blood was then mixed with progressive increments of purified bovine prothrombin. When the concentration of prothrombin was equivalent to normal the whole blood clotting time and the prothrombin time were normal. The purified prothrombin supplied all that was essential and did not add detectable amounts of extraneous pro coagulant power. The residual prothrombin in the serum was generally higher when clotting occurred in silicone lined test tubes than in glass. In silicone tubes very little hemophilia B (factor IX, autoprothrombin II) activity developed. This activity was found in the glass tubes in a concentration proportional to the original prothrombin added. The transformation of prothrombin to autoprothrombin II occurred in plasma when there was a glass surface.

* This investigation was supported by a research grant HE 05141-05 from the National Heart Institute, National Institutes of Health, TL S. Public Health Service.


 
  • References

  • 1 Mammen E. F, Thomas W. R, Seegers W. H. Activation of purified prothrombin to autoprothrombin I or autoprothrombin II (platelet cofactor II) or autoprothrombin II-A. Thrombos. Diathes. haemorrh. (Stuttg.) 5: 218 1960;
  • 2 Marciniak E, Seegers W. H. Autoprothrombin C.: A second enzyme from prothrombin. Canad. J. Biochem. 40: 597 1962;
  • 3 Seegers W. H, Cole E. R, Harmison C. R, Marciniak E. Purification and some properties of autoprothrombin C. Canad. J. Biochem. 41: 1047 1963;
  • 4 Seegers W. H, Cole E. R, Aoki N, Harmison C. R. Separation of autoprothrombin III from bovine prothrombin preparations. Canad. J. Biochem. 42: 229 1964;
  • 5 Seegers W. H. Enzyme theory of blood clotting. Fed. Proc. 23: 749 1964;
  • 6 Seegers W. H, Kagami M. The separation of autoprothrombin Ic from bovine prothrombin preparations. Canad. J. Biochem. 42: 1249 1964;
  • 7 Seegers W. H. The purification of prothrombin. Bec. Chem. Progress 13: 143 1952;
  • 8 Seegers W. H, Smith H. P. Factors which influence the activity of purified thrombin. Amer. J.Physiol. 137: 348 1942;
  • 9 Seegers W. H. Prothrombin. Harvard University Press; Cambridge, Mass.: 1962: 529
  • 10 Ware A. G, Seegers W. H. Two-stage procedure for the quantitative determination of prothrombin concentration. Amer. J. clin. Path. 19: 471 1949;
  • 11 Seegers W. H, Miller K. D, Andrews E. B, Murphy R. C. Fundamental interactions and effect of storage, ether, absorbants and blood clotting on plasma antithrombin activity. Amer. J. Physiol. 169: 700 1952;
  • 12 Seegers II W, Marciniak E. Inhibition of autoprothrombin C activity with plasma. Nature 193: 1188 1962;
  • 13 Marciniak E. Autoprothrombin activities in serum. Bull. Acad. poi. Sci. 9: 381 1961;
  • 14 Seegers W. H, Schröer H, Kagami M. Inactivation of purified autoprothrombin I with antithrombin. Canad. J. Biochem. 42: 1425 1964;
  • 15 Koller F, Baer P, Geiger M. Über die Auslösung des GerinnungsVorganges. Acta haemat. (Basel) 18: 33 1957;
  • 16 Aoki N, Harmison C. R, Seegers W. H. Properties of bovine Ac-globulin concentrates and methods of preparation. Canad. J. Biochem. 41: 2409 1963;