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Science 13 April 1979:
Vol. 204. no. 4389, pp. 200 - 202
DOI: 10.1126/science.155308
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Articles

Science, Vol 204, Issue 4389, 200-202
Copyright © 1979 by American Association for the Advancement of Science

articles

Fibrinopeptide B and aggregation of fibrinogen

Shainoff JR and BN Dardik

Removal of fibrinopeptide B from human fibrinogen by reaction with the procoagulant enzyme from copperhead snake venom below 25 degrees C resulted in tight aggregation of the fibrinogen, which, in turn, progressively blocked a concomitant but sluggish release of fibrinopeptide A by the enzyme. When the clots obtained at less than 25 degrees C were warmed, they dissociated into soluble aggregates and monomers. Release of fibrinopeptide A then resumed, and a secondary coagulation followed. The aggregation induced by release of fibrinopeptide B itself involves a plasmin-susceptible segment located just distal to B in the B beta chain of fibrinogen, a segment previously shown to be of little importance in the aggregation induced by release of fibrinopeptide A.


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