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. 1973 Apr;131(4):791–797. doi: 10.1042/bj1310791

The preparation of activated Factor X and its action on prothrombin

Jolyon Jesty 1,*, M Peter Esnouf 1
PMCID: PMC1177539  PMID: 4737325

Abstract

The preparation of activated Factor X from reaction mixtures of bovine Factor X and Russell's-viper venom is described. The molecular weight of purified protein varies about a mean value of 40000; this variation is the result of at least two forms of Factor Xa. The action of activated Factor X, together with purified Factor V, was studied on purified prothrombin and the reaction products were isolated. In addition to thrombin, two other polypeptides with molecular weights of 16000 and 19500 were recovered.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Aronson D. L., Mustafa A. J., Finlayson J. S. Two forms of the human prothrombin converting enzyme (active factor X). Proc Soc Exp Biol Med. 1971 Sep;137(4):1262–1266. doi: 10.3181/00379727-137-35769. [DOI] [PubMed] [Google Scholar]
  2. Baker W. J., Seegers W. H. The conversion of prethrombin to thrombin. Thromb Diath Haemorrh. 1967 Feb 28;17(1-2):205–213. [PubMed] [Google Scholar]
  3. Barton P. G., Jackson C. M., Hanahan D. J. Relationship between factor V and activated factor X in the generation of prothrombinase. Nature. 1967 May 27;214(5091):923–924. doi: 10.1038/214923a0. [DOI] [PubMed] [Google Scholar]
  4. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  5. DENSON K. W. The specific assay of Prower-Stuart factor and factor VII. Acta Haematol. 1961 Feb;25:105–120. doi: 10.1159/000206523. [DOI] [PubMed] [Google Scholar]
  6. Esnouf M. P., Jobin F. The isolation of factor V from bovine plasma. Biochem J. 1967 Mar;102(3):660–665. doi: 10.1042/bj1020660. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Esnouf M. P., Lloyd P. H., Jesty J. A method for the simultaneous isolation of factor X and prothrombin from bovine plasma. Biochem J. 1973 Apr;131(4):781–789. doi: 10.1042/bj1310781. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Jobin F., Esnouf M. P. Coagulant activity of tiger snake (Notechis scutatus scutatus) venom. Nature. 1966 Aug 20;211(5051):873–875. doi: 10.1038/211873b0. [DOI] [PubMed] [Google Scholar]
  9. Jobin F., Esnouf M. P. Studies on the formation of the prothrombin-converting complex. Biochem J. 1967 Mar;102(3):666–674. doi: 10.1042/bj1020666. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Leveson J. E., Esnouf M. P. The inhibition of activated Factor X with di: isopropyl fluorophosphate. Br J Haematol. 1969 Aug;17(2):173–178. doi: 10.1111/j.1365-2141.1969.tb01356.x. [DOI] [PubMed] [Google Scholar]
  11. Mann K. G., Heldebrant C. M., Fass D. N. Multiple active forms of thrombin. I. Partial resolution, differential activities, and sequential formation. J Biol Chem. 1971 Oct 10;246(19):5994–6001. [PubMed] [Google Scholar]
  12. Mann K. G., Heldebrant C. M., Fass D. N. Multiple active forms of thrombin. II. Mechanism of production from prothrombin. J Biol Chem. 1971 Oct 10;246(19):6106–6114. [PubMed] [Google Scholar]
  13. Milstone J. H., Oulianoff N., Saxton T. R., Milstone V. K. Partial and selective inactivation of thrombokinase by chymotrypsin. Yale J Biol Med. 1971 Feb-Apr;43(4-5):223–235. [PMC free article] [PubMed] [Google Scholar]
  14. PAPAHADJOPOULOS D., HANAHAN D. J. OBSERVATIONS ON THE INTERACTION OF PHOSPHOLIPIDS AND CERTAIN CLOTTING FACTORS IN PROTHROMBIN ACTIVATOR FORMATION. Biochim Biophys Acta. 1964 Aug 19;90:436–439. doi: 10.1016/0304-4165(64)90220-x. [DOI] [PubMed] [Google Scholar]
  15. Rosenberg R. D., Waugh D. F. Multiple bovine thrombin components. J Biol Chem. 1970 Oct 10;245(19):5049–5056. [PubMed] [Google Scholar]
  16. SCHWERT G. W., TAKENAKA Y. A spectrophotometric determination of trypsin and chymotrypsin. Biochim Biophys Acta. 1955 Apr;16(4):570–575. doi: 10.1016/0006-3002(55)90280-8. [DOI] [PubMed] [Google Scholar]
  17. SEEGERS W. H., COLE E. R., HARMISON C. R., MARCINIAK E. Purification and some properties of autoprothrombin C. Can J Biochem Physiol. 1963 Apr;41:1047–1063. [PubMed] [Google Scholar]
  18. Seegers W. H., Marciniak E., Kipfer R. D., Yasunaga K. Isolation and sme properties of prethrombin and autoprothrombin III. Arch Biochem Biophys. 1967 Aug;121(2):372–383. doi: 10.1016/0003-9861(67)90090-2. [DOI] [PubMed] [Google Scholar]
  19. Seegers W. H., Murano G., McCoy L. Structural changes in prothrombin during activation: a theory. Thromb Diath Haemorrh. 1970 Feb 28;23(1):26–36. [PubMed] [Google Scholar]
  20. WILLIAMS W. J., ESNOUF M. P. The fractionation of Russell's-viper (Vipera russellii) venom with special reference to the coagulant protein. Biochem J. 1962 Jul;84:52–62. doi: 10.1042/bj0840052. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]

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