Download PDF
Thromb Haemost 1964; 12(02): 355-367
DOI: 10.1055/s-0038-1655620
Originalarbeiten – Original Articles – Travaux Originaux
Schattauer GmbH

A Study of the Coagulant Action of Eight Snake Venoms[*]

Linda Nahas   **
1   Medical Research Council, Blood Coagulation Research Unit, Churchill Hospital, Oxford, U. K.
,
K. W. E Denson
1   Medical Research Council, Blood Coagulation Research Unit, Churchill Hospital, Oxford, U. K.
,
R. G Macfarlane
1   Medical Research Council, Blood Coagulation Research Unit, Churchill Hospital, Oxford, U. K.
› Author Affiliations
Further Information

Publication History

Publication Date:
27 June 2018 (online)

    Permissions and Reprints

Summary

An investigation of the eight coagulant snake venoms has revealed the presence in three of these of both a direct thrombin-like activity and the ability to produce a powerful prothrombin activator from factor X in the presence of phospholipid and factor V. The use of antivenom prepared against the venoms indicated that the active principles were antigenically distinct in the genera studied but that some species cross reaction occurred.

* Received the following grants: 1. British Council Bursary; 2. Research Fund of Instituto Butantan grant; 3. Campanha Nacional de Aperfeicoa Mento de Pessoal de Nivel Superior (Capes) -grant.


** Present address: Instituto Butantan, Caixa Postal 65, S. Paulo, Brazil.


 

  • References

  • 1 Biggs R, Douglas A. S, Macfariane R. G. The action of thromboplastic substances. J. Physiol. 122: 554 1963;
    PubMedGoogle Scholar
  • 2 Biggs R, Macfarlane R. G. Human Blood Coagulation and Its Disorders. 3rd Edition.. Black-well Scientific Publications; Oxford: 1962
    Google Scholar
  • 3 Denson K. W. Electrophoretic studies of the Prower factor: A blood coagulation factor which differs from factor VII. Brit. J. Haemat. 4: 313 1958;
    CrossrefPubMedGoogle Scholar
  • 4 Denson K. W. The specific assay of Prower-Stuart factor and factor VII. Acta Haemat. 25: 105 1961;
    CrossrefPubMedGoogle Scholar
  • 5 Esnouf M. P, Williams W. J. The isolation and purification of a bovine-plasma protein which is a substrate for the coagulant fraction of Russell’s viper venom. Biochem. J. 84: 62 1962;
    CrossrefPubMedGoogle Scholar
  • 6 Ferguson J. H, Wilson Ennis E. G. Enzymes and blood clotting. II. Antiprothrombin C, Russell’s viper venom (Stypven), and Trypsin. Thrombos. Diathes. haemorrh. (Stuttg.) 9: 62 1963;
    PubMedGoogle Scholar
  • 7 Fullerton H. W. Estimation of prothrombin. Lancet II: 195 1940;
    PubMedGoogle Scholar
  • 8 Henrigues O. B, Fishnau M, Henriques S. B. Partial purification and some properties of blood coagulation factor from the venom of Bothrops jararaca. Biochem. J. 75: 551 1960;
    CrossrefPubMedGoogle Scholar
  • 9 Hougie C. Effect of Russell’s viper venom (Stypven) on Stuart clotting defect. Proc. Soc. exp. Biol. 93: 570 1956;
    CrossrefPubMedGoogle Scholar
  • 10 Macfarlane R. G. The coagulant action of Russell’s viper venom: the use of antivenom in defining its reaction with a serum factor. Brit. J. Haemat. 7: 496 1961;
    CrossrefPubMedGoogle Scholar
  • 11 Macfarlane R. G, Barnett B. The haemostatic possibilities of snake venom. Lancet 11: 985 1934;
    PubMedGoogle Scholar
  • 12 Peden J. C, Peacock A. C. The coagulation of blood by Russell’s viper venom. A reaction between Russell’s viper venom and beef serum factors. J. Lab. clin. Med. 52: 101 1958;
    PubMedGoogle Scholar
  • 13 Rechnic J, de Vries A, Perlwertter C, Levi C, Kochwa S, Gitter S. Coagulation factors in the venoms of Vipera palestinae and Echis colorata. A preliminary report. Bull. Res. Coun. Israel E 8: 81 1960;
    PubMedGoogle Scholar
  • 14 Rosenfeld J, Hampe O. G, Kelen E. M. A. Coagulant and fibrinolytic activity of animal venoms; determination of coagulant and fibrinolytic index of different species. Mem. Inst. Butantan 29: 143 1959;
    PubMedGoogle Scholar
  • 15 Williams W. J, Esnouf M. P. The fractionation of Russell’s viper venom (Vipera Russellii) with special reference to the coagulant protein. Biochem. J. 84: 52 1962;
    CrossrefPubMedGoogle Scholar