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The major clot-forming substrate in the blood plasma of vertebrates. Though fibrinogen represents a small fraction of plasma proteins (normal human...

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Figure 1.Fibrinogen models. (a) Computer image of the symmetrical molecule. (b) Model for end-to-end aggregation. (c) Half-staggered molecular overlap between side-to-side aggregated filaments in a clot network. (Parts a and b from C. Cohen et al., The structure of fibrinogen and fibrin, pt. I, Ann. N. Y. Acad. Sci., 408:194–213, 1983; c from J. S. Weisel, G. N. Phillips, Jr., and C. Cohen, pt. II, Ann. N. Y. Acad. Sci., 408:367–378, 1983)

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Figure 2.Physiological pathway for the clotting of fibrinogen in normal plasma. Clotting time is measured by forming the (fibrin)n network; this, however, is not the end product. Unless this clot undergoes ligation by ?-glutamyl-e-lysine cross-links, bleeding may ensue. Such disorders of fibrin stabilization occur in the hereditary absence of factor XIII or when inhibitors to one of the reaction steps (marked 1–3) appear in the blood circulation. (After T. H. Spaet, ed., Progress in Hemostasis and Thrombosis, vol. 5, pp. 245–290, Grune and Stratton, 1980)

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Figure 3.Formation of ?-glutamyl-e-lysine peptide bridges between fibrin molecules is the last enzyme-catalyzed reaction in blood clotting.

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