Download PDF
Thromb Haemost 1963; 09(01): 053-061
DOI: 10.1055/s-0038-1654960
Originalarbeiten — Original Articles — Travaux Originaux
Schattauer GmbH

Procoagulant Material From Human Urine in Prothrombin Activation[*]

M June Caldwell
1   Department of Physiology and Pharmacology, Wayne State University, College of Medicine, Detroit, Michigan, USA, and From the Department of Medicine, University of Colorado, School of Medicine, and Belle Bonfils Memorial Blood Bank, Denver, Colorado, USA
,
Kurt N von Kaulla
1   Department of Physiology and Pharmacology, Wayne State University, College of Medicine, Detroit, Michigan, USA, and From the Department of Medicine, University of Colorado, School of Medicine, and Belle Bonfils Memorial Blood Bank, Denver, Colorado, USA
,
Edith von Kaulla
1   Department of Physiology and Pharmacology, Wayne State University, College of Medicine, Detroit, Michigan, USA, and From the Department of Medicine, University of Colorado, School of Medicine, and Belle Bonfils Memorial Blood Bank, Denver, Colorado, USA
,
Walter H Seegers
1   Department of Physiology and Pharmacology, Wayne State University, College of Medicine, Detroit, Michigan, USA, and From the Department of Medicine, University of Colorado, School of Medicine, and Belle Bonfils Memorial Blood Bank, Denver, Colorado, USA
› Author Affiliations
Further Information

Publication History

Publication Date:
21 June 2018 (online)

Also available at
    Permissions and Reprints

Summary

The procoagulant or P fraction obtained from human urine was analyzed to determine how it functions in the activation of purified prothrombin. Prothrombin converts to thrombin in the presence of P fraction, Ac-globulin, calcium chloride and either whole platelets or platelet factor 3. The yield of thrombin can be made to depend upon the concentration of P fraction. This conversion of prothrombin to thrombin can be partially or completely inhibited by adding various concentrations of soybean trypsin inhibitor introduced into the activation mixture.

When purified prothrombin was activated with platelet factor 3 and calcium chloride, the prothrombin activity, as measured by the two-stage assay, decreased. When it was at the lowest possible level, P fraction was added. Quite quickly prothrombin activity began to reappear, and soon 100% of the original prothrombin activity was accounted for as either prothrombin-R or thrombin.

* At Wayne State University this work was supported by a research grant H-5141 from the National Heart Institute, National Institutes of Health, U. S. Public Health Service, and at the University of Colorado by grant H-5538 and The Belle Bonfils Memorial Blood Bank, Denver.


 

  • References

  • 1 Tocantins L. M, Lindquist J. N. Thromboplastic Activity of the Urine. Proc. Soc. exp. Biol. (N. Y) 65: 44 1947;
    CrossrefPubMedSearch in Google Scholar
  • 2 Grunke W. Studien über die Blutgerinnung mit besonderer Berücksichtigung der Hämophile. Z. ges. exp. Med. 96: 512 1935;
    CrossrefPubMedSearch in Google Scholar
  • 3 von Kaulla K. N. Urokinase-Induced Fibrinolysis of Human Standard Clots. Nature 183: 1320 1959;
    CrossrefPubMedSearch in Google Scholar
  • 4 von Kaulla K. N. Extraction and Concentration of Thromboplastic Material from Human Urine. Proc. Soc. exp. Biol. (N. Y) 91: 543 1956;
    CrossrefPubMedSearch in Google Scholar
  • 5 von Kaulla K. N. Methods for Preparation of Purified Human Thromboplastin and Fibrinolysokinase from Urine. Acta haemat. (Basel) 16: 315 1956;
    CrossrefPubMedSearch in Google Scholar
  • 6 Hecht E. R, Cho M. H, Seegers W. H. Thromboplastin: Nomenclature and Preparation of Protein-Free Material Different from Platelet Factor 3 or Lipid Activator. Amer. J. Physiol. 193: 584 1958;
    PubMedSearch in Google Scholar
  • 7 Alkjaersig N, Seegers W. H. Formation of Prothrombin from Autoprothrombin by Means of Liver Mitochondria. Amer. J. Physiol. 183: 111 1955;
    PubMedSearch in Google Scholar
  • 8 Barnhart M. I. Partial Activation of Prothrombin and Generation of Prothrombin-R with Cathepsin B. Amer. J. Physiol. 198: 899 1960;
    PubMedSearch in Google Scholar
  • 9 Ware A. G, Seegers W. H. Two-stage Procedure for the Quantitative Determination of Prothrombin Concentration. Amer. J. Clin. Path. 19: 471 1949;
    PubMedSearch in Google Scholar
  • 10 Seegers W. H, Smith H. P. Factors which Influences the Activity of Purified Thrombin. Amer. J. Physiol. 137: 348 1942;
    PubMedSearch in Google Scholar
  • 11 Seegers W. H. Prothrombin. Harvard University Press; Cambridge, Massachusetts: 1962
    Search in Google Scholar
  • 12 Seegers W. H. The Purification of Prothrombin. Rec. Chem. Progress 13: 143 1952;
    PubMedSearch in Google Scholar
  • 13 Alkjaersig N, Abe T, Seegers W. H. Purification and Quantitative Determination of Platelet Factor 3. Amer. J. Physiol. 181: 304 1955;
    PubMedSearch in Google Scholar
  • 14 Cole E. R, Marciniak E, Seegers W. H. Procedures for the Quantitative Determination of Autoprothrombin C. Thrombos. Diathes. haemorrh. 08: 434 1962;
    PubMedSearch in Google Scholar
  • 15 Shulman S, Landaburu R. H, Seegers W. H. Biophysical Studies on Platelet Cofactor I Preparations. Thrombos. Diathes. haemorrh. 04: 336 1960;
    PubMedSearch in Google Scholar
  • 16 Mertz E. T, Seegers W. H, Smith H. P. Prothrombin, Thromboplastin, and Thrombin: Quantitative Interrelationships. Proc. Soc. exp. Biol. (N. Y) 42: 604 1939;
    CrossrefPubMedSearch in Google Scholar
  • 17 Glendening M. B, Page E. W. The Site of Inhibition of Blood Clotting by Soy Bean Trypsin Inhibitor. J. Clin. Invest 30: 1298 1951;
    CrossrefPubMedSearch in Google Scholar
  • 18 Alkjaersig N, Deutsch E, Seegers W. H. Prothrombin Derivatives and the Inhibition of Thrombin Formation with Soy Bean Trypsin Inhibitor. Amer. J. Physiol. 180: 367 1955;
    PubMedSearch in Google Scholar