Soluble Fibrin Complexes in Early Fibrin Digests*

Luddo B. Nanninga

doi:10.1055/s-0038-1649219

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1977; 37(02): 192-200
DOI: 10.1055/s-0038-1649219

Original Article

Schattauer GmbH

Soluble Fibrin Complexes in Early Fibrin Digests*

Luddo B. Nanninga

¹Department of Physiology and Biophysics, University of Texas Medical Branch Galveston, Texas 77550, USA

› Author Affiliations

Abstract

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Summary

Early fibrin digests were analyzed in the ultracentrifuge and were found to contain compounds with molecular weights up to 3 x 10⁶; these compounds are considered to be soluble fibrin complexes. Their similarity with intermediate polymers in inhibited clotting systems has been stressed. Their viscosity at low shear rates is extremely high; therefore, a rapid method to establish their presence in plasma would be the measurement of plasma and serum viscosity at low shear rates. Moreover, they shorten the clotting time (thrombin time) of fibrinogen considerably.

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References

References
1 Astrup T. Role of blood coagulation and fibrinolysis in the pathogenesis of arteriosclerosis. In: Page I.H. (Ed.) Connective Tissue, Thrombosis and Atherosclerosis Aca demic Press; 1959: p. 223
2 Bang N.U, Hansen M.S, Smith G.F, Mosesson M.W. Properties of soluble fibrin polymers encountered in thrombotic states. Thrombosis et Diathesis Haemorrhagica Suppl 1973; 56: 75
3 Beller F.K, Maki M. Properties of fibrinogenolysis and fibrinolysis products in immune assays. Thrombosis Diathesis Haemorrhagica 1967; 18: 114
4 Bettelheim F.R. The clotting of fibrinogen. II. Fractionation of peptide material liberated. Biochimica Biophysica Acta 1956; 19: 121
5 Blombäck B, Blombäck M. The molecular structure of fibrinogen. Annals New York Academy of Sciences 1972; 202: 77
6 Copley A.L. Fibrinolysis and Atherosclerosis. Lancet 1957; I: 102
7 Edsall J.T, Foster J.F, Scheinberg H. Studies on double refraction of flow. III. Human fibrinogen and fraction I of human plasma. Journal American Chemical Society 1947; 69: 2731
8 Ehrlich P, Shulman S, Ferry J.D. The conversion of fibrinogen to fibrin. VIII Sedimentation and viscosity studies on clotting systems inhibited by urea and solutions of fibrin in urea. Journal American Chemical Society 1952; 74: 2258
9 Ferry J.D, Shulman S, Gutfreund K, Katz S. The conversion of fibrinogen to fibrin. XI. Lightscattering studies on clotting systems inhibited by hexamethyleneglycol. Journal American Chemical Society 1952; 74: 5709
10 Fletcher A.P, Alkjaersig N, Sherry S. Pathogenesis of the coagulation defect developing during pathological plasma proteolytic (fibrinolytic) states. I. The significance of fibrinogen proteolysis and circulating fibrinogen degradation products. Journal of Clinical Investigation 1962; 41: 896
11 Fletcher A.P, Alkjaersig N, O’Brien J, Tulevski V.J. Blood hypercoagulability and thrombosis. Transactions American Association of Physicians 1970; 83: 159
12 Fletcher A.P, Alkjaersig N. Blood hypercoagulability, intravascular coagulation and thrombosis. New diagnostic concepts. Thrombosis et Diathesis Haemorrhagica Suppl. 1971; 45: 389
13 Fletcher A.P, Alkjaersig N. Blood screening methods for the diagnosis of thrombosis. Millbank Memorial Fund Quarterly, 50, Part 1972; 2: 171
14 Gormsen J, Laursen B. Fibrinogen breakdown products and clotting parameters. Thrombosis Diathesis Haemorrhagica 1967; 17: 467
15 Graeff H, von Hugo R. Fibrinogen derivatives with a higher molecular weight than that of the parent molecule in cord vein plasma of newborns. I. Identification in single plasma samples. Klinische Wochenschrift 1973; 51: 695
16 Green H.D. Circulatory system: physical principles. In: Glasser O. Medical Physics 1950; 2: 228
17 Gurewich V, Niewiarowski S, Hutchinson E. The detection of fibrin degradation products. Application of the serial dilution protamine sulfate (SDPS) test to fibrinolytic therapy. Thrombosis et Diathesis Haemorrhagica Suppl. 1971; 47: 137
18 Hansen M.S, Bang N.U, Barton R.D, Mattler L.E. Enhancement of blood coagulation by soluble fibrin complexes. Journal of Experimental Medicine 1975; 141: 944
19 Hocking C.S, Laskowski Jr. M, Scheraga H.A. Size and shape of bovine fibrinogen. Journal American Chemical Society 1952; 74: 775
20 von Hugo R, Graeff H. Fibrin-i degradation products with a molecular weight higher than that of fibrinogen. Identification and characterization of in vitro products from human plasma. Thrombosis et Diathesis Haemorrhagica 1973; 29: 122
21 von Hugo R, Graeff H. Identifizierung und Präparation von hochmolekularen Derivaten des Fibrinogens aus Humanplasma durch PAA-Gelelektrophorese and Agarose-Gelchromatographie. Thrombosis et Diathesis Haemorrhagica Supp. 1974; 55: 325
22 Kalbfleisch J.M, Bird R.M. Cryofibrinogenemia. New England Journal of Medicine 1960; 263: 881
23 Katz S, Gutfreund K, Shulman S, Ferry J.D. The conversion of fibrinogen to fibrin. X. Lightscattering studies of bovine fibrinogen. Journal American Chemical Society 1952; 74: 5706
24 Kierulf P. Studies on soluble fibrin in plasma. III. N-Terminal analysis of a modified fraction I (Cohn) from patient plasmas. Scandinavian Journal of Clinical and Laboratory Investigation 1973; 31: 37
25 Kierulf P. Studies on soluble fibrin in plasma. III. N-Terminal analysis of a modified fraction I (Cohn) from plasmin and thrombin-incubated plasma. Scandinavian Journal Clinical and Laboratory Investigation 1973; 31: 43
26 Kopec M, Wegrzynowicz Z, Budzynski A.Z, Latallo Z.S, Kowalski E. Interaction of fibrinogen degradation products (FDP) with platelets. Experimental Biology and Medicine 1968; 3: 73
27 Kopec M, Wegrzynowicz Z, Latallo Z.S. Effects of some basic proteins and acid mucopolysaccharides on fibrin deposition. Thrombosis Diathesis Haemorrhagica Suppl. 1970; 40: 253
28 Kopec M, Wegrzynowicz Z, Latallo Z.S. Soluble fibrin complexes and a new specific test for their detection. Thrombosis Diathesis Haemorrhagica Suppl. 1970; 39: 219
29 Korst D.R, Kratochvil C.H. Cryofibrinogen in a case of lung neoplasm associated with thrombophlebitis migrans. Blood 1955; 10: 945
30 Landis W.J, Waugh D.F. Interactions of bovine fibrinogen and thrombin. Archives Biochemistry and Biophysics 1975; 168: 498
31 Laurent T.C, Blombäck B. On the significance of the release of two different peptides from fibrinogen during clotting. Acta Chemica Scandinavica 1958; 12: 1875
32 Lewis J.H, Wilson J.H. Fibrinogen breakdown products. American Journal Physiology 1964; 207: 1053
33 Lipinski B, Budzynski A.Z, Latallo Z.S, Kowalski E. Isolation and characterization or cold insoluble fibrinogen complexes from bovine plasma. Acta Biochemica Polonica 1964; 9: 527
34 Lipinski B, Wegrzynowicz Z, Budzynski A.Z, Kopec M, Latallo Z.S, Kowalski E. Soluble unclottable complexes formed in the presence of fibrinogen degradation products (FDP) during the fibrinogen-fibrin conversion and their potential significance in pathology. Thrombosis Diathesis Haemorrhagica 1967; 17: 65
35 Lipinski B, Worowski K. Detection of soluble fibrin monomer complexes in blood by means of protamine sulfate test. Thrombosis et Diathesis Haemorrhagica 1968; 20: 44
36 Lipinski B, Kotelba-Witkowska B, Zajdel M. The level of soluble fibrin monomer complexes in blood of healthy humans. Abstracts International Congress of Hematology, Munich 1970: p. 74
37 McKee P.A, Kalbfleisch J.M, Bird R.M. Incidence and significance of cryofibrinogenemia. Journal of Laboratory and Clinical Medicine 1963; 61: 203
38 Marder V.J, Shulman N.R, Carroll W.R. The importance of intermediate degradation products of fibrinogen in fibrinolytic hemorrhage. Transactions American Association Physicians 1967; 80: 156
39 Marder V.J, Shulman N.R. High molecular weight derivatives of human fibrinogen produced by fibrinolysin. II. Mechanism of their anticoagulant activity. Journal of Biological Chemistry 1969; 244: 2120
40 Maxwell R.E, Nickel V.S, Lewandowski V. Preparations of plasminogen deficient fibrinogen and thrombin. Biochemical Biophysical Research Communications 1962; 7: 50
41 Merrill E.W, Cokelet G.C, Britten A, Wells Jr. R.E. Non-Newtonian rheology of human blood-effect of fibrinogen deduced by “subtraction”. Circulation Research 1963; 13: 48
42 Nanninga L.B. Fibrinogen preparation, photoelectric determination molecular weight and viscosity, formal titration before and after clotting. Archives Neerlandaises de Physiologie de l’homme et des Animaux 1946; 28: 241
43 Nanninga L.B. Molar concentrations of fibrinolytic components, especially free fibrinolysin in vivo. Thrombosis Diathesis Haemorrhagica 1975; 33: 244
44 Niewiarowski S, Gurewich V. Laboratory identification of intravascular coagulation. The serial dilution protamine sulfate test for the detection of fibrin monomer and fibrin degradation products. Journal Laboratory and Clinical Medicine 1971; 77: 665
45 Nowak A, Lipinski B, Drzewiecki J. Levels of soluble fibrin monomer complexes in the course of myocardial infarction. British Heart Journal 1972; 34: 593
46 Oncley J.L, Scatchard G, Brown A. Physicochemical characteristics of certain of the proteins of normal human plasma. Journal Physical and Colloid Chemistry 1947; 51: 184
47 Ritzman S.E, Levin W.C. Cryopathies, a review. Archives of Internal Medicine 1961; 107: 186
48 Schachman H.K. Ultracentrifugation, diffusion and viscometry. Methods in Enzymology 1957; 4: 32
49 Scheraga H.A, Backus J.K. Flow birefringence in arrested clotting systems. Journal American Chemical Society 1952; 74: 1979
50 Sherman L.A, Harwig S, Lee J. In vitro formation and in vivo clearance of fibrinogen-fibrin complexes. Journal of Laboratory and Clinical Medicine 1975; 86: 100
51 Shulman S. The size and shape of bovine fibrinogen. Studies of sedimentation, diffusion and viscosity. Journal American Chemical Society 1953; 75: 5846
52 Smith G.F, Bang N.U. Formation of soluble fibrin polymers. Fibrin degradation fragments D and E fail to form soluble complexes with fibrin monomer. Biochemistry 1972; 11: 2958
53 Staudinger H. Organische Kolloidchemie Ed. Vieweg; Braunschweig: 1940
54 Tinoco Jr. I, Ferry J.D. The conversion of fibrinogen to fibrin XV. Sedimentation studies of the polymer of fibrinogen at high pH. Archives of Biochemistry and Biophysics 1954; 48: 7
55 Wells Jr. R.E, Gawronski T.H, Cox P.J, Perrera R.D. Influence of fibrinogen on flow properties of erythrocyte suspensions. American Journal of Physiology 1964; 207: 1035