Cross-linked gamma-chains in a fibrin fibril are situated transversely between its strands.
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.
Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, 1054 BRB II/III, 421 Curie Blvd, Philadelphia, PA 19104-6058, USA. weisel@cellbio.med.upenn.edu
J W
JW
Weisel
D018360:Crystallography, X-Ray; D005337:Fibrin / Q000737:chemistry* / Q000648:ultrastructure*; D005342:Fibrinolysis; D006801:Humans; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013223:Statistics as Topic / Q000379:methods
D046911:Macromolecular Substances; D005337:Fibrin