Thromb Haemost 1977; 37(02): 201-209
DOI: 10.1055/s-0038-1649220
Original Article
Schattauer GmbH

The Half-Life of Plasmic Degradation Products of Human Fibrinogen in Rabbits

N Ardaillou
1   Department of Coagulation (U.143, I.N.S.E.R.M.), Institut de Pathologie Cellulaire, Hôpital de Bicêtre, 94270 Le Kremlin-Bicêtre, France
,
L Dray
1   Department of Coagulation (U.143, I.N.S.E.R.M.), Institut de Pathologie Cellulaire, Hôpital de Bicêtre, 94270 Le Kremlin-Bicêtre, France
,
A. Z Budzynski
*   Department of Medicine and the Specialized Center of Research in Thrombosis, Temple University Health Sciences Center, Philadelphia, Pennsylvania
,
V. J Marder
*   Department of Medicine and the Specialized Center of Research in Thrombosis, Temple University Health Sciences Center, Philadelphia, Pennsylvania
,
M. J Larrieu
1   Department of Coagulation (U.143, I.N.S.E.R.M.), Institut de Pathologie Cellulaire, Hôpital de Bicêtre, 94270 Le Kremlin-Bicêtre, France
› Author Affiliations
Further Information

Publication History

Received 14 June 1976

Accepted 14 October 1976

Publication Date:
24 July 2018 (online)

Summary

Human fibrinogen and purified plasmic degradation fragments X (stages 1 and 2), D and E were labelled with 125-1 using the lactoperoxidase method. The chromatographic, elec-trophoretic and immunologic properties of the labelled proteins were found to be similar to those of non-labelled fragments. All the degradation products diffused rapidly (T½ 0.27–0.75 hours) from the intravascular space of rabbits, as compared with fibrinogen (4.26 hours). In addition, the metabolic half-life was found to be 49.3 hours for fibrinogen, as compared with only 5.1, 6.1, 2.3 and 1.4 for fragments X (stage 1), X (stage 2), D and E, respectively. The metabolic half-life roughly reflects the molecular size of the degradation products.

 
  • References

  • 1 Alkjaersig N, Fletcher A.P, Sherry S. Pathogenesis of the coagulation defect developing during pathological plasma proteolytic (“fibrinolytic”) states. II. The significance mechanism and consequences of defective fibrin polymerization. Journal of Clinical Investigation 1962; 41: 917
  • 2 Ardaillou N, Larrieu M.J. In vitro studies of radio-iodinated fibrinogen. Comparison of the ICI and enzymatic methods. Thrombosis Research 1974; 5: 327
  • 3 Ardaillou N, Sraer J.D, Beaufils P. Fibrinogen kinetics in chronic renal failure of various causes. Biomedicine 1974; 21: 49
  • 4 Atencio A.C, Bailey H.R, Reeve E.B. Studies on the metabolism and distribution of fibrinogen in young and older rabbits. I. Methods and models. Journal of Laboratory and Clinical Medicine 1965; 66: 1
  • 5 Budzynski A.J, Marder V.J, Shainoff J.R. Structure of plasmic degradation products of human fibrinogen. The Journal of Biological Chemistry 1974; 249: 2294
  • 6 Catanzaro A, Edgington T.S. The in vivo behavior of the terminal derivatives of fibrinogen and fibrin cleaved by plasmin. Journal of Laboratory and Clinical Medicine 1974; 83: 458
  • 7 Collen D, Tytgatt G.N, Claeys H, Piessens R. Metabolism and distribution of fibrinogen. I. Fibrinogen turnover in physiological conditions in humans. British Journal of Haematology 1972; 22: 681
  • 8 Haynes O.A, Sherman L.A. In vivo behavior of fibrinogen fragment D in experimental renal, hepatic and reticuloendothelial dysfunction. American Journal of Pathology 1973; 71: 219
  • 9 Jamieson G.A, Gaffney P.J. Heterogeneity of fibrin polymerization inhibitor. Biochimica et Biophysica Acta 1966; 121: 217
  • 10 Jamieson G.A, Gaffney P.J. Nature of the high molecular weight fraction of fibrinolytic digests of human fibrinogen. Biochimie et Biophysica Acta 1968; 154: 96
  • 11 Latallo Z.S, Budzynski A.Z, Lipinski B, Kowalski E. Inhibition of thrombin and fibrin polymerization. Two activities derived from plasmin digested fibrinogen. Nature 1964; 203: 1184
  • 12 Larrieu M.J, Rigollot C, Marder V.J. Comparative effects of fibrinogen degradation Fragments D and E on coagulation. British Journal of Haematology 1972; 22: 719
  • 13 McFarlane A.S, Todd D, Cromwell S. Fibrinogen catabolism in humans. Clinical Science 1964; 26: 415
  • 14 Marder V.J, Budzynski A.Z. The structure of the fibrinogen degradation products. In: Spaet T. (Edit.) Progress in Hemostasis and Thrombosis 1974; vol. 2: p. 141
  • 15 Marder V.J, James H.L, Sherry S. The purification of fibrinogen degradation products by Pevikon block electrophoresis. Thrombosis Diathesis Haemorrhagica 1969; a 22: 234
  • 16 Marder V.J, Shulman N.R, Carroll W.R. High molecular weight derivatives of human fibrinogen produced by plasmin. I. Physiochemical and immunological characterization. Journal of Biological Chemistry 1969; b 244: 2111
  • 17 Miyachi Y, Vaitukaitis J.L, Nieschlag E, Lipsett M.B. Enzymatic radioiodination of gonadotropins. Journal of Clinical Endocrinology and Metabolism 1972; 34: 23
  • 18 Mosesson M.W. Fibrinogen catabolic path ways. Seminars in Thrombosis and Hemostasis 1974; 1: 63
  • 19 Otis P.T, Rapaport S.I. Failure of fibrinogen degradation products to increase plasma fibrinogen in rabbits. Proceedings of the Society for Experimental Biology and Medicine 1973; 144: 124
  • 20 Piessens R, Collen D, Tytgatt G.N. Computer analysis of fibrinogen tracer data. Computer and Biomedical Research 1971; 4: 585
  • 21 Ratnoff O.D, Menzie A. A new method for the determination of fibrinogen in small samples of plasma. Journal of Laboratory and Clinical Medicine 1951; 37: 316
  • 22 Regoeczi E. Iodine-labelled fibrinog: A review. British Journal of Haematology 1971; 20: 649
  • 23 Scheidegger J.J. Une microméthode de l’immunoélectrophorèse. Internal Archives of Allergy and applied immunology 1955; 7: 103
  • 24 Sherman L.A. Fibrinogen turnover: Demonstration of multiple pathways of catabolism. Journal of Laboratory and Clinical Medicine 1972; 79: 710
  • 25 Tranqui-Pouit L, Marder V.J, Suscillon M, Budzynski A.Z, Hudry-Clergeon G. Electron microscopic studies of plasmic degradation products of fibrinogen. Biochimica et Biophysica Acta 1975; 400: 189
  • 26 Tytgatt G.N, Collen D, Verstraete M. Metabolism of fibrinogen in cirrhosis of the liver. Journal of Clinical Investigation 1971; 50: 1690
  • 27 Weber K, Osborn M. The reliability of molecular weight determinations by dodecyl sul-fate-polyacrylamide gel electrophoresis. Journal of Biological Chemistry 1969; 244: 4406