Download PDF
Thromb Haemost 1975; 34(02): 455-464
DOI: 10.1055/s-0038-1651404
Original Article
Schattauer GmbH

Studies on PIVKA-X

Gustav Gaudernack
1   Institute of Medical Biology, University of Tromsø, Tromsø, Norway
,
Hans Prydz
1   Institute of Medical Biology, University of Tromsø, Tromsø, Norway
› Author Affiliations
Further Information

Publication History

Received 13 December 1974

Accepted 19 May 1975

Publication Date:
02 July 2018 (online)

Also available at
    Permissions and Reprints

Summary

The incorporation of 14C-glucosamine and 3H-leucine into PIVKA-X and factor X has been studied in Macaca mulatta by means of a monospecific precipitating antiserum. No difference in the incorporation into PIVKA-X and factor X was found.

The half-lives of PIVKA-X and factor X were similar (about 30-35 h and 27-31 h respectively) indicating that the vitamin K-induced modifications did not alter the survival of protein.

A Russell’s-viper venom/cephalin test system for factor X was more sensitive to inhibition by PIVKA-X than was a tissue thromboplastin-based system.

 

  • References

  • 1 Gaudernack G, Gladhaug Berre Â, Østerud B, and Prydz H. 1974; Immunological Studies on the Blood Coagulation Factor X and Its Warfarin-Induced Precursor. Thrombosis et Diathesis Haemorrhagica 31: 40.
    PubMedSearch in Google Scholar
  • 2 Gladhaug Â, and Prydz H. 1970; Purification of the Coagulation Factors VII and X from Human Serum. Some Properties of Factor VII. Biochimica et Biophysica Acta 215: 105.
    CrossrefPubMedSearch in Google Scholar
  • 3 Gladhaug Berre Â, Østerud B, Christensen T. B, Holm T, and Prydz H. 1973; Some Characteristics of the Coagulation Factor Xa purified from Human Serum. Biochemical Journal 135: 791.
    CrossrefPubMedSearch in Google Scholar
  • 4 Hemker H. C, and Muller A. D. 1968; Kinetic Aspects of the Interaction of Blood Clotting Enzymes. VI. Localization of the Site of Blood-coagulation Inhibition by the Protein induced by Vitamin K Absence (PIVKA). Thrombosis et Diathesis Haemorrhagica 20: 78.
    PubMedSearch in Google Scholar
  • 5 Hjort P. F, Rapaport S. I, and Owren P. A. 1955; A Simple, Specific One-stage Prothrombin Assay using Russell’s viper venom in Cephalin Suspension. Journal of Laboratory and Clinical Medicine 46: 89.
    PubMedSearch in Google Scholar
  • 6 Hjort P. F. 1957; Intermediate Reactions in the Coagulation of Blood with Tissue Thromboplastin. Convertin, Accelerin, Prothrombinase. Scandinavian Journal of Clinical and Laboratory Investigation 9: 27
    PubMedSearch in Google Scholar
  • 7 Johnson H. V, Martinovic J, and Johnson B. C. 1971; Vitamin K and the Biosynthesis of the Glycoprotein Prothrombin. Biochemical and Biophysical Research Communication 43: 1040.
    CrossrefPubMedSearch in Google Scholar
  • 8 Lowry O. H, Rosebrough N. J, Farr A. L, and Randall R. J. 1951; Protein measurements with the Folin phenol reagent. Journal of Biological Chemistry 193: 265.
    PubMedSearch in Google Scholar
  • 9 Magnusson S, Sottrup-Jensen L, Petersen T. E, Morris H. R, and Dell A. 1974; Primary Structure of the Vitamin K-Dependent Part of Prothrombin. FEBS Letters 44: 189.
    CrossrefPubMedSearch in Google Scholar
  • 10 Nelsestuen G. L, and Suttie J. W. 1972; The Purification and Properties of an Abnormal Prothrombin Protein Produced by Dicumarol-treated Cows. Journal of Biological Chemistry 247: 8176.
    PubMedSearch in Google Scholar
  • 11 Nelsestuen G. L, and Suttie J. W. 1973; The Mode of Action of Vitamin K. Isolation of a Peptide containing the Vitamin K-dependent Portion of Prothrombin. Proceedings of the National Academy of Sciences U.S.A 70: 3366.
    CrossrefPubMedSearch in Google Scholar
  • 12 Paus P. N. 1973 On Rapidly Labeled RNA from Rat Liver. A methodological and biological study. Thesis, University Press, Oslo.
    PubMedSearch in Google Scholar
  • 13 Pereira M, and Couri D. 1971; Studies on the Site of Action of Dicumarol on Prothrombin Biosynthesis. Biochimica et Biophysica Acta 237: 348.
    CrossrefPubMedSearch in Google Scholar
  • 14 Pereira M, and Couri D. 1972; Site of Inhibition by Dicumarol of Prothrombin Biosynthesis: Carbohydrate Content of Prothrombin from Dicumarol-treated Rats. Biochimica et Biophysica Acta 261: 375.
    CrossrefPubMedSearch in Google Scholar
  • 15 Prydz H, and Gladhaug Â. 1971; Factor X. Immunological Studies. Thrombosis et Diathesis Haemorrhagica 25: 157.
    PubMedSearch in Google Scholar
  • 16 Prydz H. 1974. Biosynthesis of the Factors of the Prothrombin Complex. In: Brinkhous K. M, and Hinnon S. (eds.) Thrombosis: Pathogenesis and Clinical Trials. F.K. Schattauer Verlag; Wien:
    Search in Google Scholar
  • 17 Stenflo J, Fernlund P, Engan W, and Roepstorff P. 1974; Vitamin K Dependent Modifications of Glutamic Acid Residues in Prothrombin. Proceedings of the National Academy of Sciences U.S.A 71: 2730.
    CrossrefPubMedSearch in Google Scholar
  • 18 Stenflo J. 1974; Vitamin K and the Biosjmthesis of Prothrombin. IV. Isolation of Peptides Containing Prosthetic Groups from Normal Prothrombin and the Corresponding Peptides from Dicumarol-induced Prothrombin. Journal of Biological Chemistry 249: 5527.
    PubMedSearch in Google Scholar