Cross-linked gamma-chains in a fibrin fibril are situated transversely between its strands

J Thromb Haemost. 2004 Aug;2(8):1467-9; discussion 1469-73. doi: 10.1111/j.1538-7836.2004.00873.x.

Abstract

There is no evidence for the change from transverse to longitudinal orientation hypothesized to explain X-ray and electron microscope structures. Dissolution of the clot through fibrinolysis to produce soluble products is difficult to reconcile with transverse cross-linking. There are flaws in the interpretation supporting transverse cross-linking of experiments with fibrin as a template and stretching. In summary, the strongest evidence from X-ray crystallography, fibrinolysis, and electron microscopy experiments favors the presence of longitudinal cross-links in fibrin.

Publication types

  • Comment

MeSH terms

  • Crystallography, X-Ray
  • Fibrin / chemistry*
  • Fibrin / ultrastructure*
  • Fibrinolysis
  • Humans
  • Macromolecular Substances
  • Microscopy, Electron
  • Protein Conformation
  • Protein Structure, Secondary
  • Statistics as Topic / methods

Substances

  • Macromolecular Substances
  • Fibrin