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. 1983 Mar;80(6):1570–1573. doi: 10.1073/pnas.80.6.1570

Band patterns seen by electron microscopy in ordered arrays of bovine and human fibrinogen and fibrin after negative staining.

R C Williams
PMCID: PMC393643  PMID: 6572920

Abstract

When fibers of fibrin clots or fragments of fibrinogen pellets are negatively stained they exhibit in the electron microscope characteristic patterns of cross-striations or bands. Those found in pellet material are indistinguishable from those seen in thrombin-induced fibrin fibers. The pattern seen in fibrin from bovine sources contains three equally spaced faint bands between every two of the broad prominent ones, spaced 23 nm apart. Human material shows a different pattern, one wherein no central faint band is seen, whereas the two remaining ones are broader. Its character is unaffected by crosslinking following fiber formation and preceding negative staining. The bovine pattern, however, is converted by such crosslinking to one that closely resembles the human. It is suggested that the striation pattern in human fibrin is due to juxtapositions of E domains of the parallel-aligned fibrin monomers with tightly coiled COOH-terminal regions of beta and gamma polypeptide chains, with no discernible contribution to the pattern from the alpha chain. In negatively stained untreated fibers of bovine fibrin, however, it is proposed that the COOH-terminal region of the alpha chain becomes tightly coiled, thereby contributing the faint central striation to the band pattern. Crosslinking prevents this conformational change in the alpha chain.

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Selected References

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

  1. Belitser V. A., Manjakov V. P., Varetskaja T. V. Medium-dependent structure modifications of reconstituting fibrin. Biochim Biophys Acta. 1971 Jun 29;236(3):546–549. doi: 10.1016/0005-2795(71)90238-8. [DOI] [PubMed] [Google Scholar]
  2. COHEN C., REVEL J. P., KUCERA J. Paracrystalline forms of fibrinogen. Science. 1963 Aug 2;141(3579):436–438. doi: 10.1126/science.141.3579.436. [DOI] [PubMed] [Google Scholar]
  3. Cohen C., Slayter H., Goldstein L., Kucera J., Hall C. Polymorphism in fibrinogen aggregates. J Mol Biol. 1966 Dec 28;22(2):385–386. doi: 10.1016/0022-2836(66)90144-6. [DOI] [PubMed] [Google Scholar]
  4. Fowler W. E., Hantgan R. R., Hermans J., Erickson H. P. Structure of the fibrin protofibril. Proc Natl Acad Sci U S A. 1981 Aug;78(8):4872–4876. doi: 10.1073/pnas.78.8.4872. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hantgan R., Fowler W., Erickson H., Hermans J. Fibrin assembly: a comparison of electron microscopic and light scattering results. Thromb Haemost. 1980 Dec 19;44(3):119–124. [PubMed] [Google Scholar]
  6. Karges H. E., Kühn K. The cross striation pattern of the fibrin fibril. Eur J Biochem. 1970 May 1;14(1):94–97. doi: 10.1111/j.1432-1033.1970.tb00265.x. [DOI] [PubMed] [Google Scholar]
  7. Kay D., Cuddigan B. J. The fine structure of fibrin. Br J Haematol. 1967 May;13(3):341–347. doi: 10.1111/j.1365-2141.1967.tb08749.x. [DOI] [PubMed] [Google Scholar]
  8. Mosesson M. W., Hainfeld J., Wall J., Haschemeyer R. H. Identification and mass analysis of human fibrinogen molecules and their domains by scanning transmission electron microscopy. J Mol Biol. 1981 Dec 15;153(3):695–718. doi: 10.1016/0022-2836(81)90414-9. [DOI] [PubMed] [Google Scholar]
  9. STRYER L., COHEN C., LANGRIDGE R. Axial period of fibrinogen and fibrin. Nature. 1963 Feb 23;197:793–794. doi: 10.1038/197793a0. [DOI] [PubMed] [Google Scholar]
  10. Stewart G. J., Niewiarowski S. Nonenzymatic polymerization of fibrinogen by protamine sulfate. An electron microscope study. Biochim Biophys Acta. 1969 Dec 23;194(2):462–469. doi: 10.1016/0005-2795(69)90106-8. [DOI] [PubMed] [Google Scholar]
  11. Tooney N. M., Cohen C. Crystalline states of a modified fibrinogen. J Mol Biol. 1977 Feb 25;110(2):363–385. doi: 10.1016/s0022-2836(77)80077-6. [DOI] [PubMed] [Google Scholar]
  12. Tooney N. M., Cohen C. Microcrystals of a modified fibrinogen. Nature. 1972 May 5;237(5349):23–25. doi: 10.1038/237023a0. [DOI] [PubMed] [Google Scholar]
  13. Weisel J. W., Phillips G. N., Jr, Cohen C. A model from electron microscopy for the molecular structure of fibrinogen and fibrin. Nature. 1981 Jan 22;289(5795):263–267. doi: 10.1038/289263a0. [DOI] [PubMed] [Google Scholar]
  14. Williams R. C. Morphology of bovine fibrinogen monomers and fibrin oligomers. J Mol Biol. 1981 Aug 15;150(3):399–408. doi: 10.1016/0022-2836(81)90555-6. [DOI] [PubMed] [Google Scholar]
  15. Yamanaka G., Glazer A. N., Williams R. C. Cyanobacterial phycobilisomes. Characterization of the phycobilisomes of Synechococcus sp. 6301. J Biol Chem. 1978 Nov 25;253(22):8303–8310. [PubMed] [Google Scholar]

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