Thrombosis and Haemostasis, Table of Contents Thromb Haemost 1967; 17(03/04): 440-451DOI: 10.1055/s-0038-1654169 Originalarbeiten - Original Articles - Travaux Originaux Schattauer GmbH Preparation and Properties of Anticoagulant Split Product of Fibrinogen and Its Determination in Plasma[*] L. B Nanninga 1 Department of Physiology, University of Texas, Medical Branch, Galveston, Texas , M. M Guest ** 1 Department of Physiology, University of Texas, Medical Branch, Galveston, Texas › Author Affiliations Recommend Article Abstract Buy Article Summary The anticoagulant split product resulting from fibrinolytic digestion was found by two independent methods to be 83% by weight of the initial fibrinogen. Molecular weights of the fibrinogen and the two split products were determined. A method for purification of the anticoagulant split product is described and a quantitative method to estimate this product in plasma is presented. A virtual absence of this split product was found in normal plasma, while it appeared in large amounts after fibrinolytic activation. Observations on the inhibition of clotting by the split product and blocking of the inhibition by positive dyes are presented. A similarity between the inhibition of clotting by this product and by negative dyes is suggested. Full Text References References 1 Niewiarowski S, Kowalski E. Un nouvel anticoagulant dérivé du fibrinogène. Revue Hémat 13: 321 1958; 2 Triantaphyllopoulos D. C. Anticoagulant effect of incubated fibrinogen. Canad. J. Biochem 315: 249 1958; 3 Seegers W. H, Nieft M. L, Vandenbelt J. M. Decomposition products of fibrinogen and fibrin. Arch. Biochem 7: 15 1945; 4 Nussenzweig V, Seligmann M, Pelmont J, Grabar P. Les Produits de dégradation du fibrinogène humain par la plasmine. I. Separation et propriétés physicochimiques. Ann. Inst. Pasteur 100: 317 1961; 5 Triantaphyllopoulos E, Triantaphyllopoulos D. C. Variability of the anticoagulant fraction of incubated fibrinogen. Amer. J. Physiol 208: 52 1965; 6 Jamieson G. A, Pert J. H. Studies on the digestion of human fibrinogen with plasmin. Vox Sang 5: 460 1963; 7 Ware A. G, Guest M. M, Seegers W. H. Fibrinogen : with special reference to its preparation and certain properties of the product. Arch. Biochem 13: 231 1947; 8 Nanninga L. B, Guest M. M. On the interaction of fibrinolysin (plasmin) with the inhibitors antifibrinolysin and soybean trypsin inhibitor. Arch. Biochem 108: 542 1964; 9 Mihalyi E, Godfrey J. E. Digestion of fibrinogen by trypsin. Characterization of the large fragment obtained. Biochim. biophys. Acta (Amst.) 67: 90 1963; 10 Marx R, Weinzierl W, Schwick G, Sterike K. Zum Nachweis und Vorkommen und zur Bedeutung intracorporal entstandener Fibrin(ogen) Abbauprodukte mit besonderer Berücksichtigung des Nachweises von hochmolekularen Fibrinabbauprodukten im Menstrualblut. Blut 12: 22 1965; 11 Steichele D. F, Herschiein H. J, Woerner I. Das Serumeiweißbild der geburtshilflichen Afibrinogenämie, Dysproteinämie infolge ungerinnbarer Fibrinogen derivate. Klin. Wschr 44: 228 1966; 12 Maki M, Kikuchi I, Watanabe S, Kikuchi E. A coagulation anomaly; plasma being made non-clottable by adding thrombin and clottable by thromboplastin-calcium or Toluidine Blue-Thrombin. Tohoku J. exp. Med 84: 274 1965; 13 Ferreira H. G, Murat L. G. An immunological method for demonstrating fibrin degradation products in serum and its use in the diagnosis of fibrinolytic states. Brit. J. Haematology 2: 299 1963; 14 Bang N. U, Fletcher A. P, Alkjaersig N, Sherry S. Pathogenesis of the coagulation defect developing during pathological plasma proteolytic (fibrinolytic) states. III. Demonstration of abnormal clot structure by electron microscopy. 15 Batallo Z. S, Fletcher A. P, Alkjaersig N, Sherry S. Inhibition of fibrin polymerization by fibrinogen proteolysis products. Amer. J. Physiol 203: 68 1962; 16 Nanninga L. B. Unpublished experiments. 17 Schachman H. K. Ultracentrifugation, diffusion and viscometry. Methods in Enzymology IV: 32 1957;
