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

[1]  W. Nieuwenhuizen,et al.  Anticoagulant And Calcium-Binding Properties Of High Molecular Weight Derivatives Of Human Fibrinogen, Produced By Plasmin (Fragments X) , 1981, Thrombosis and Haemostasis.

[2]  J. Shainoff,et al.  Role of fibrinogen in fibrin transport: chromatographic studies. , 1980, Thrombosis research.

[3]  G. Kemp,et al.  The presence of A Ca2+ bridge within the γ chain of human fibrinogen , 1979 .

[4]  J. Hermans,et al.  Early events in the plasmin digestion of fibrinogen and fibrin. Effects of plasmin on fibrin polymerization. , 1977, The Journal of biological chemistry.

[5]  F. Haverkate,et al.  Protective effect of calcium in the plasmin degradation of fibrinogen and fibrin fragments D. , 1977, Thrombosis research.

[6]  N. Bang,et al.  Analysis of soluble fibrin complexes by agarose gel chromatography and protamine sulfate gelation. , 1976, Biochimica et biophysica acta.

[7]  N. Ardaillou,et al.  Biological Effects of Fibrinogen-Fibrin Degradation Products , 1975, Thrombosis and Haemostasis.

[8]  V. Belitser,et al.  Enhanced anticlotting activity of fragments D formed during plasmin hydrolysis of fibrinogen in the presence of calcium chloride. , 1975, Thrombosis research.

[9]  V. Marder,et al.  Electron microscopic studies of plasmic degradation products of fibrinogen. Implications for the disulfide structure of fibrinogen. , 1975, Biochimica et biophysica acta.

[10]  L. Pouit,et al.  Models proposed for the fibrinogen molecule and for the polymerization process. , 1975, Thrombosis research.

[11]  V. Marder,et al.  Structure of plasmic degradation products of human fibrinogen. Fibrinopeptide and polypeptide chain analysis. , 1974, The Journal of biological chemistry.

[12]  D. Wallach,et al.  Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. , 1971, Biochemistry.

[13]  K. Weber,et al.  The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. , 1969, The Journal of biological chemistry.

[14]  V. Marder,et al.  High molecular weight derivatives of human fibrinogen produced by plasmin. II. Mechanism of their anticoagulant activity. , 1969, The Journal of biological chemistry.

[15]  V. Marder,et al.  High molecular weight derivatives of human fibrinogen produced by plasmin. I. Physicochemical and immunological characterization. , 1969, The Journal of biological chemistry.

[16]  M. Stahl,et al.  High molecular weight products of the late stage of fibrinogen proteolysis by plasmin and their structural relation to the fibrinogen molecule. , 1967, Biochimica et biophysica acta.

[17]  L. Goldstein,et al.  Polymorphism in fibrinogen aggregates. , 1966, Journal of molecular biology.

[18]  A. Budzynski,et al.  Inhibition of Thrombin and of Fibrin Polymerization, Two Activities derived from Plasmin-digested Fibrinogen , 1964, Nature.

[19]  Oliver H. Lowry,et al.  Protein measurement with the Folin phenol reagent. , 1951, The Journal of biological chemistry.

[20]  T. Ugarova,et al.  On the properties of fibrin monomer prepared from fibrin clot with acetic acid. , 1979, Thrombosis research.

[21]  Varetskaia Tv,et al.  Anticlotting activity of fragment D from fibrinogen and fibrin and its dependence on calcium presence when fragments are obtained from fibrinogen , 1976 .

[22]  V. Marder,et al.  The importance of intermediate degradation products of fibrinogen in fibrinolytic hemorrhage. , 1967, Transactions of the Association of American Physicians.