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Molecular Aspects of Fibrin Clot Solubilization

Nature New Biology volume 234, pages 281–282 (1971)Cite this article

Abstract

THE human plasma protein, fibrinogen, is a disulphide bonded1 dimer2, each unit containing an Aα, Bβ and 8 chain*, interconnected by disulphide bridges3. Thrombin (E.C.3.4.4.-13) releases fibrinopeptides A and B from the Aα and Bβ chains respectively4 to form fibrin monomer (α2β2γ2) † which polymerizes to form fibrin polymer or clotted fibrin. This polymer, following factor XIII (plasma transglutaminase, fibrin stabilizing factor) mediated crosslinking among the α chains and among the γ chains5, is one of the major and initiating constituents of a thrombus. Fibrinolytic activators, for example, streptokinase (SK) and urokinase (UK), are of thrombolytic value as they convert the thrombus plasminogen to plasmin (E.C.3.4.4.14) which by fibrinolytic action dissolves the thrombus. Whereas the interaction of fibrinogen and plasmin has been well studied6–9, little is known concerning the mechanism of plasmin mediated fibrin clot lysis. I report here on the mechanism of non-cross-linked fibrin clot solubilization in near physiological conditions.

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  1. National Institute for Medical Research, Mill Hill, London, NW7 1AA

    PATRICK J. GAFFNEY

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  1. PATRICK J. GAFFNEY
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GAFFNEY, P. Molecular Aspects of Fibrin Clot Solubilization. Nature New Biology 234, 281–282 (1971). https://doi.org/10.1038/newbio234281a0

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