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Studies on a procoagulant fraction of southern copperhead snake venom: The preferential release of fibrinopeptide B

  • Roger H. Herzig
    Footnotes
    Affiliations
    From the Department of Medicine, Case Western Reserve University School of Medicine, University Hospitals of Cleveland, Cleveland, Ohio U.S.A.

    From the Research Division of the Cleveland Clinic Foundation Cleveland, Ohio U.S.A.
    Search for articles by this author
  • Oscar D. Ratnoff
    Correspondence
    Reprint requests: Dr. Oscar D. Ratnoff, University Hospitals of Cleveland, Cleveland, Ohio 44106.
    Footnotes
    Affiliations
    From the Department of Medicine, Case Western Reserve University School of Medicine, University Hospitals of Cleveland, Cleveland, Ohio U.S.A.

    From the Research Division of the Cleveland Clinic Foundation Cleveland, Ohio U.S.A.
    Search for articles by this author
  • John R. Shainoff
    Affiliations
    From the Department of Medicine, Case Western Reserve University School of Medicine, University Hospitals of Cleveland, Cleveland, Ohio U.S.A.

    From the Research Division of the Cleveland Clinic Foundation Cleveland, Ohio U.S.A.
    Search for articles by this author
  • Author Footnotes
    ∗ This study was performed in partial fulfillment for the degree of Doctor of Medicine, Case Western Reserve University.
    ∗∗ Career Investigator of the American Heart Association.
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      Abstract

      The venom of the southern copperhead snake (Ancistrodon contortrix contortrix) possesses procoagulant and fibrinolytic properties. A procoagulant fraction, separated by chromatography and gel filtration, clotted fibrinogen directly and possessed proteolytic, esterolytic, and amidase activities. In its action upon fibrinogen, the fraction released fibrinopeptide B at a much faster rate than fibrinopeptide A, the reverse of the effect of thrombin. Despite the rapid release of fibrinopeptide B, visible clotting did not take place until appreciable fibrinopeptide A was also removed. These experiments support the view that visible clotting depends upon the removal of fibrinopeptide A from the fibrinogen molecule, permitting aggregation of monomeric units.
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