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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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Article info
Publication history
Accepted:
July 2,
1970
Received:
May 25,
1970
Footnotes
☆This study was supported in part by Research Grants HE 01661 and HE 06835 from the National Heart and Lung Institute of the National Institutes of Health, the United States Public Health Service, and in part by grants from the American Heart Association.
Identification
Copyright
© 1970 Published by Elsevier Inc.