Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1979 Mar;76(3):1461–1463. doi: 10.1073/pnas.76.3.1461

Amidolytic properties of single-chain activated Hageman factor.

O D Ratnoff, H Saito
PMCID: PMC383272  PMID: 286331

Abstract

Activation of Hageman factor (Factor XII) upon exposure to negatively charged agents has been attributed to proteolytic cleavage of this molecule. To examine this question, purified Hageman factor was exposed to Sephadex gels to which ellagic acid had been adsorbed. Such Hageman factor, separated from the gels and studied in the fluid phase, was amidolytic. Nonetheless, no cleavage of Hageman factor treated in this way could be demonstrated by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. Thus, activation of Hageman factor by negatively charged agents was not necessarily accompanied by molecular scission.

Full text

PDF
1461

Selected References

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

  1. Cochrane C. G., Revak S. D., Wuepper K. D. Activation of Hageman factor in solid and fluid phases. A critical role of kallikrein. J Exp Med. 1973 Dec 1;138(6):1564–1583. doi: 10.1084/jem.138.6.1564. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Cochrane C. G., Wuepper K. D. The first component of the kinin-forming system in human and rabbit plasma. Its relationship to clotting factor XII (Hageman Factor). J Exp Med. 1971 Oct 1;134(4):986–1004. doi: 10.1084/jem.134.4.986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Donaldson V. H., Ratnoff O. D. Hageman factor: alterations in physical properties during activation. Science. 1965 Nov 5;150(3697):754–756. doi: 10.1126/science.150.3697.754. [DOI] [PubMed] [Google Scholar]
  4. Fair B. D., Saito H., Ratnoff O. D., Rippon W. B. Detection by fluorescence of structural changes accompanying the activation of Hageman factor (factor XII). Proc Soc Exp Biol Med. 1977 Jun;155(2):199–202. doi: 10.3181/00379727-155-39773. [DOI] [PubMed] [Google Scholar]
  5. Fujikawa K., Kurachi K., Davie E. W. Characterization of bovine factor XIIa (activated Hageman factor). Biochemistry. 1977 Sep 20;16(19):4182–4188. doi: 10.1021/bi00638a008. [DOI] [PubMed] [Google Scholar]
  6. McMillin C. R., Saito H., Ratnoff O. D., Walton A. G. The secondary structure of human Hageman factor (factor XII) and its alteration by activating agents. J Clin Invest. 1974 Dec;54(6):1312–1322. doi: 10.1172/JCI107877. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Prentice C. R., Ratnoff O. D., Breckenridge R. T. Experiments on the nature of the prothrombin-converting principle: alteration of proaccelerin by thrombin. Br J Haematol. 1967 Nov;13(6):898–914. doi: 10.1111/j.1365-2141.1967.tb08860.x. [DOI] [PubMed] [Google Scholar]
  8. Ratnoff O. D., Saito H. Interactions among Hageman factor, plasma prekallikrein, high molecular weight kininogen, and plasma thromboplastin antecedent. Proc Natl Acad Sci U S A. 1979 Feb;76(2):958–961. doi: 10.1073/pnas.76.2.958. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Ratnoff O. D. Studies on the product of the reaction between activated Hageman factor (factor XII) and plasma thromboplastin antecedent (factor XI). J Lab Clin Med. 1972 Nov;80(5):704–710. [PubMed] [Google Scholar]
  10. Revak S. D., Cochrane C. G., Bouma B. N., Griffin J. H. Surface and fluid phase activities of two forms of activated Hageman factor produced during contact activation of plasma. J Exp Med. 1978 Mar 1;147(3):719–729. doi: 10.1084/jem.147.3.719. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Revak S. D., Cochrane C. G., Griffin J. H. The binding and cleavage characteristics of human Hageman factor during contact activation. A comparison of normal plasma with plasmas deficient in factor XI, prekallikrein, or high molecular weight kininogen. J Clin Invest. 1977 Jun;59(6):1167–1175. doi: 10.1172/JCI108741. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Revak S. D., Cochrane C. G., Johnston A. R., Hugli T. E. Structural changes accompanying enzymatic activation of human Hageman factor. J Clin Invest. 1974 Sep;54(3):619–627. doi: 10.1172/JCI107799. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Saito H. Purification of high molecular weight kininogen and the role of this agent in blood coagulation. J Clin Invest. 1977 Sep;60(3):584–594. doi: 10.1172/JCI108810. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Saito H., Ratnoff O. D., Donaldson V. H. Defective activation of clotting, fibrinolytic, and permeability-enhancing systems in human Fletcher trait plasma. Circ Res. 1974 May;34(5):641–651. doi: 10.1161/01.res.34.5.641. [DOI] [PubMed] [Google Scholar]
  15. Saito H., Ratnoff O. D., Donaldson V. H., Haney G., Pensky J. Inhibition of the adsorption of Hagemen factor (Factor XII) to glass by normal human plasma. J Lab Clin Med. 1974 Jul;84(1):62–73. [PubMed] [Google Scholar]
  16. Saito H., Ratnoff O. D. Inhibition of normal clotting and Fletcher factor activity by rabbit anti-kallikrein antiserum. Nature. 1974 Apr 12;248(449):597–598. doi: 10.1038/248597a0. [DOI] [PubMed] [Google Scholar]
  17. Soltay M. J., Movat H. Z., Ozge-Anwar A. H. The kinin system of human plasma. V. The probable derivation of prekallikrein activator from activated Hageman factor (XIIa). Proc Soc Exp Biol Med. 1971 Dec;138(3):952–958. doi: 10.3181/00379727-138-36026. [DOI] [PubMed] [Google Scholar]
  18. Soltay M. J., Movat H. Z., Ozge-Anwar A. H. The kinin system of human plasma. V. The probable derivation of prekallikrein activator from activated Hageman factor (XIIa). Proc Soc Exp Biol Med. 1971 Dec;138(3):952–958. doi: 10.3181/00379727-138-36026. [DOI] [PubMed] [Google Scholar]
  19. 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]
  20. Zimmerman T. S., Ratnoff O. D., Powell A. E. Immunologic differentiation of classic hemophilia (factor 8 deficiency) and von Willebrand's dissase, with observations on combined deficiencies of antihemophilic factor and proaccelerin (factor V) and on an acquired circulating anticoagulant against antihemophilic factor. J Clin Invest. 1971 Jan;50(1):244–254. doi: 10.1172/JCI106480. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES