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Thromb Haemost 1969; 22(01): 001-012
DOI: 10.1055/s-0038-1651323
Originalarbeiten-Original Articles-Travaux Originaux
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On the in Vivo Clearance of Thrombin[*]

H Gans
1   Department of Surgery, the New York Hospital-Cornell University Medical College, New York, New York, 10021
,
R Stern
1   Department of Surgery, the New York Hospital-Cornell University Medical College, New York, New York, 10021
,
B. H Tan
1   Department of Surgery, the New York Hospital-Cornell University Medical College, New York, New York, 10021
› Author AffiliationsSupported by U. S. Public Health Service Grants, HE 05341 and HE 12324 and a N. I. H. Research Career Program Award.
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Publication History

Publication Date:
10 June 2018 (online)

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Summary

The turnover of labeled bovine thrombin was studied in heparinized dogs. The results of these studies indicate that

1. thrombin is rapidly removed from the blood, clearance takes place predominantly by the liver ;

2. the uptake occurs by the Kupffer cells ;

3. after its uptake the thrombin is rapidly broken down ;

4. in the absence of the liver thrombin is slowly cleared by extrahepatic phagocytes ;

5. the rate of thrombin clearance is so rapid and its critical dose so small that this protein can be used to study hepatic blood flow and Kupffer cell clearance function.

* The first part of this paper was presented at the Sixteenth Symposium on Blood, January 19-20, 1968, Detroit; the second part at the Fifth National Scientific Meeting of the Reticuloendothelial Society, New York, December 1—4, 1968.


 

  • References

  • 1 Quick A. J. Is Heparin An Antiprothrombin?. Proc. Soc. exp. Biol. (N. Y.) 35: 391 1936;
    CrossrefPubMedGoogle Scholar
  • 1a Astrup T. Heparin and the Inhibition of Blood Clotting. Science 90: 36 1939;
    PubMedGoogle Scholar
  • 1b Brinkhous K. M, Smith H. P, Warner E. D, Seegers W. H. Heparin and Blood Clotting. Science 90: 539 1939;
    PubMedGoogle Scholar
  • 2 Foa C. Sulle Leggi d’Azione della Trombina. Arch, di Fisiol. 10: 479 1912;
    PubMedGoogle Scholar
  • 2a Seegers W. H, Nieft M, Loomis E. C. Note on the Adsorption of Thrombin on Fibrin. Science 101: 520 1945;
    CrossrefPubMedGoogle Scholar
  • 2b Quick A. J, Favre Gilly J. Fibrin, A Factor Influencing the Consumption of Prothrombin in Coagulation. Amer. J. Phys. 158: 387 1949;
    CrossrefPubMedGoogle Scholar
  • 3 Gans H, Subramanian V, Tan B. H. Selective Phagocytosis: A New Concept in Protein Catabolism. Science 159: 107 1968;
    CrossrefPubMedGoogle Scholar
  • 4 McFarlane A.S. In Vivo Behavior of I131 Fibrinogen. J. clin. Inv. 42: 346 1963;
    CrossrefPubMedGoogle Scholar
  • 5 Miller K. D, Copeland W. H. Isolation of Human Thrombin. Proc. Soc. exp. Biol. (N. Y.) 111: 512 1962;
    CrossrefPubMedGoogle Scholar
  • 6 Gans H. Study of Mechanisms which Preserve Blood Fluidity and the Effect of their Inhibition on Thrombogenesis. J. Surg. Res. 6: 87 1966;
    CrossrefPubMedGoogle Scholar
  • 7 Gans H. Study of Fibrinogen Turnover Rates after Total Hepatectomy in Dogs. Surgery 55: 544 1964;
    PubMedGoogle Scholar
  • 8 Gans H, Lowman J. T. The Uptake of Fibrin and Fibrin-Degradation Products by the Isolated Perfused Rat Liver. Blood 29: 526 1967;
    PubMedGoogle Scholar
  • 9 Biozzi G, Holpern B. N, Stiffel C, Mouton D. Quantitative Study of the Metabolic Activity of the Kupffer Cells on a Heat-Denatured Serum Albumin Labeled with I131 . Brit. J. exp. Path. 59: 510 1958;
    PubMedGoogle Scholar
  • 9a Palmer D. L, Rifkind D, Brown D. I131-Labeled Colloidal Human Serum Albumin in the Study of Reticuloendothelial System Function: The Distribution of Free and Colloid-Bound Radioiodide. J. Lab. clin. Med. 68: 972 1966;
    PubMedGoogle Scholar
  • 10 Gordon A. H. The Use of the Isolated Perfused Liver to Detect Alterations to Plasma Proteins. Biochem. J. 66: 255 1957;
    CrossrefPubMedGoogle Scholar
  • 11 Cohen S, Gordon A. H. Catabolism of Plasma Albumin by the Perfused Rat Liver. Biochem. J. 70: 544 1958;
    CrossrefPubMedGoogle Scholar
  • 12 Thorbecke G. J, Maurer P. H, Benacerraf B. The Affinity of the Reticuloendothelial System for Various Modified Serum Proteins. Brit. J. exp. Path. 41: 190 1960;
    PubMedGoogle Scholar