Advertisement

On the Identity of Fibrin(ogen) Oligomers Appearing during Fibrin Polymerization

  • Agnes Henschen
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 281)

Abstract

Fibrinogen (1) is a dimeric, symmetrical molecule with the overall structure (Aα, Bβ, γ)2. When fibrinogen is converted into fibrin by the action of thrombin two moles of each fibrinopeptide A and B are finally released. Hereby four N-terminal polymerization sites are revealed in each molecule and these can then interact with four pre-existing C-terminal polymerization sites so that fibrin oligomers and polymers are formed. It is well established that A-peptides are removed from fibrinogen before B-peptides and that A-peptide release alone is sufficient for clotting to occur. The two fibrin types formed have the structures [(α, β, γ)2]n and [(α, Bβ, γ)2]n respectively.

Keywords

Cyanogen Bromide Elution Pattern Soluble Oligomer Symmetrical Molecule Fibrin Polymerization 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    A. Henschen and J. McDonagh, Fibrinogen, fibrin and factor XIII, in: “Blood coagulation”, R. F. A. Zwaal and H. C. Hemker, eds., Elsevier Science Publishers, Amsterdam, (1986).Google Scholar
  2. 2.
    E. B. Hunziker, P. W. Straub and A. Haeberli, Molecular morphology of fibrin monomers and early oligomers during fibrin polymerization, J. Ultrastruct. Molec. Struct. Res., 98:60 (1988).CrossRefGoogle Scholar
  3. 3.
    G. F. Smith, Fibrinogen-fibrin conversion, Biochem. J., 185:1 (1980).PubMedGoogle Scholar
  4. 4.
    A. Visser and T. A. Payens, On the kinetics of the thrombin-controlled polymerization of fibrin, FEBS Lett., 142:35 (1982).PubMedCrossRefGoogle Scholar
  5. 5.
    N. Alkjaersig and A. P. Fletcher, Formation of soluble fibrin oligomers in purified systems and in plasma, Biochem. J.,213:75 (1983).PubMedGoogle Scholar
  6. 6.
    J. Wilf and A. P. Minton, Soluble fibrin-fibrinogen complexes as intermediates in fibrin gel formation, Biochem.,25:3124 (1986).CrossRefGoogle Scholar
  7. 7.
    M. Kehl, F. Lottspeich and A. Henschen, Analysis of human fibrinopeptides by high-performance liquid chromatography, Hoppe-Seyler’s Z. Physiol. Chem., 362:1661 (1981).PubMedGoogle Scholar
  8. 8.
    F. R. Matthias, R. Reinicke and D. L. Heene, Affinity chromatography and quantitation of soluble fibrin from plasma, Thromb. Res., 10:365 (1977).PubMedCrossRefGoogle Scholar
  9. 9.
    A. Henschen, Disulfide bridges in the middle part of fibrinogen, Hoppe-Seyler’s Z. Physiol. Chem., 359:1757 (1978).PubMedCrossRefGoogle Scholar
  10. 10.
    M. Kehl. F. Lottspeich and A. Henschen, High-performance liquid chromatography of proteins as applied to fibrinogen chains, Hoppe-Seyler’s Z. Physiol. Chem., 363:1501 (1982).PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Agnes Henschen
    • 1
  1. 1.Department of Molecular Biology and BiochemistryUniversity of California, IrvineIrvineUSA

Personalised recommendations