Quantitation of the inhibitory effect of fibrinogen and its degradation products on fibrin polymerization

• Published in: Thrombosis research Vol. 27; no. 3; pp. 261 - 269
• Main Authors: Belitser, V.A., Lugovskoy, E.V., Musjalkovskaja, A.A., Gogolinskaja, G.K.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Ltd 01.08.1982
• Subjects: Animals; Blood Coagulation; Cattle; Fibrin; Fibrin Fibrinogen Degradation Products - metabolism; Fibrin Fibrinogen Degradation Products - pharmacology; Fibrin polymerization; Fibrinogen - pharmacology; Macromolecular Substances; Platelet Membrane Glycoproteins; quantitation test; Receptors, Cell Surface; specific inhibitors; Fibrin polymerization; specific inhibitors; quantitation test
• ISSN: 0049-3848; 1879-2472
• DOI: 10.1016/0049-3848(82)90073-1

Anticlotting activities of fibrinogen and its plasmin degradation products - fragments X,Y and D - have been measured. On the molar basis fragments Y and D are found equally active whereas fragment X acts about 2 times stronger. We suggest that the inhibitory effect depends on a set of specific binding sites characteristic of domain D. As fragment X possesses two such sets its activity is twice as high as that of the single-set fragments Y and D. In spite of its two domains D fibrinogen inhibits clotting much weaker than fragment X. This is probably due to the presence in fibrinogen of large COOH-terminal sections of the two Aα-chains interfering with the inhibitory effect. The possible role of these Aα-chain sections in fibrinogen-fibrin system is discussed.