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Thromb Haemost 1959; 03(04): 491-500
DOI: 10.1055/s-0038-1654405
Originalarbeiten — Original Articles — Travaux Originaux
Schattauer GmbH

Influence of Organ Extracts on Blood Clotting Factors

P Fantl
1   Baker Medical Research Institute, Melbourne, Victoria
,
H. A Ward   *)
1   Baker Medical Research Institute, Melbourne, Victoria
› Author Affiliations
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Publication History

Publication Date:
12 June 2018 (online)

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Summary

Brain and lung suspensions incubated with blood or serum produce sera which are deficient in factor IX and factor VII.

Suspensions prepared from acetone-dehydrated brain are effective substitutes for free phospholipids in the formation of blood thromboplastin.

The fraction which inactivates the clotting factors is connected with a readily sedimentable portion of the brain suspension.

It is heat stable, and destroyed by ethanol-ether extraction.

The extracted lipid is inactive.


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*) This investigation was supported by a grant from the National Health and Medical Research Council of Australia.


  • References

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    PubMedSearch in Google Scholar
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    PubMedSearch in Google Scholar
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    PubMedSearch in Google Scholar
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    PubMedSearch in Google Scholar
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    Search in Google Scholar
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    PubMedSearch in Google Scholar
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  • References

  • 1 Sherry S, Fletcher A. P, Alkjaersig N. Fibrinolysis and fibrinolytic activity in man. Physiol. Rev 1959; 39: 343
    CrossrefPubMedSearch in Google Scholar
  • 2 Brinkhous K. M, Penick G. D. Some systemic alterations in clotting factors following local tissue injury. In "Thrombosis and Embolism." Proc. First Int. Conf. Basel, 1954. edited Koller T, Merz W. R. Basel: Benno Schwabe & Co; 1955: p. 428
    Search in Google Scholar
  • 3 Page E. W, Fulton L. D, Glendening M. B. The cause of the blood coagulation defect following abruptio placentae. Amer. J. Obstet. Gynec 1951; 61: 1116
    CrossrefPubMedSearch in Google Scholar
  • 4 Schneider C. L. Rupture of the basal (decidual) plate in abruptio placentae: A pathway of auto-extraction from the decidua into the maternal circulation. Amer. J. Obstet. Gynec 1952; 63: 1078
    CrossrefPubMedSearch in Google Scholar
  • 5 Tuller M. A. Amniotic fluid emboli and embolism. Afibrinogenemia and disseminated fibrin thrombosis: Case report and review of literature. Amer. J. Obstet. Gynec 1957; 73: 273
    CrossrefPubMedSearch in Google Scholar
  • 6 Penick G. D, Roberts H. R, Webster W. P, Brinkhous K. M. Hemorrhagic states secondary to intravascular clotting. A.M.A. Arch. Path 1958; 66: 208
    PubMedSearch in Google Scholar
  • 7 Schneider C. L. The active principle of placental toxin: thromboplastin. Its inacti-vation in blood: antithromboplastins. Amer. J. Physiol 1947; 149: 123
    PubMedSearch in Google Scholar
  • 8 Thomas L. Studies on the intravascular effect of tissue suspensions in mice. II. A factor in normal rabbit serum which inhibits the thromboplastic effect of the sedimentable tissue component. Bull. Johns Hopk. Hosp 1947; 81: 26
    PubMedSearch in Google Scholar
  • 9 Wessler S, Connelly M. T. Studies in intravascular coagulation. II. A comparison of the effect of dicumarol and heparin on clot formation in isolated venous segments. J. clin. Invest 1953; 32: 650
    CrossrefPubMedSearch in Google Scholar
  • 10 Quick A. J. The thromboplastic reagent for the determination of prothrombin. Scienc 1940; 92: 113
    PubMedSearch in Google Scholar
  • 11 Fantl P. Thrombin and the thromboplastic activity of plasma. Aust. J. exp. Biol. med. Sci 1958; 36: 581
    PubMedSearch in Google Scholar
  • 12 Biggs R, Douglas A. S. The thromboplastin generation test. J. clin. Path 1953; 6: 23
    CrossrefPubMedSearch in Google Scholar
  • 13 Fantl P. The use of substances depressing antithrombin activity in the assay of prothrombin. Biochem. J 1954; 57: 416
    CrossrefPubMedSearch in Google Scholar
  • 14 De Vries A, Alexander B, Goldstein R. A factor in serum which accelerates the conversion of prothrombin to thrombin. Bloo 1949; 4: 247
    PubMedSearch in Google Scholar
  • 15 Allen R. J. L. The estimation of phosphorus. Biochem. J 1940; 34: 858
    CrossrefPubMedSearch in Google Scholar
  • 16 Fantl P, Sawers R. J, Marr A. G. Investigation of a haemorrhagic disease due to beta-prothromboplastin deficiency complicated by a specific inhibitor of thromboplastin formation. Aust. Ann. Med 1956; 5: 163
    PubMedSearch in Google Scholar
  • 17 Flynn J. E, Coon R. W. Purification and isolation of certain intermediates formed prior to the activation of prothrombin. Amer. J. Physiol 1953; 175: 289
    PubMedSearch in Google Scholar
  • 18 McLean J. The thromboplastic action of cephalin. Amer. J. Physiol 1916; 41: 250
    PubMedSearch in Google Scholar
  • 19 Rapaport S. I, Aas K, Owren P. A. The lipid inhibitor of brain: Mechanism of its anticoagulant action and its comparison with the soybean inositolphosphatide inhibitor. J. Lab. clin. Med 1954; 44: 364
    PubMedSearch in Google Scholar
  • 20 Trethewie E. R. Clotting in heart and brain. Aust. J. exp. Biol. med. Sci 1946; 24: 185
    PubMedSearch in Google Scholar
  • 21 Tocantins L. M, Carroll R. T. Separation and assay of a lipid antithrombo-plastin from human brain, blood, plasma and plasma fractions. In Blood Clotting and Allied Problems. Transactions second. conf. Josiah Macy: Jr. Foundation; 1949: 11
    Search in Google Scholar
  • 22 Overman R. S, Wright I. S. A new blood clotting inhibitor. J. biol. Chem 1948; 174: 759
    PubMedSearch in Google Scholar
  • 23 Kingsbury K. J, Morgan D. M. Effect of ether-insoluble phosphatides on plasma recalcification times. Scand. J. clin. Lab. Invest 1958; 10: 116
    CrossrefPubMedSearch in Google Scholar

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