Abstract
Flow birefringence was observed during the polymerization process of fibrinogen catalyzed by thrombin under the experimental conditions for the formation of fine clots at a much smaller velocity gradient than in the previous observation. No flow birefringence was detected in the case of fibrinogen catalyzed by Reptilase under the corresponding conditions. This is a clear evidence implying the role of a polymerization site formed by the release of fibrinopeptide B, abbreviated as FPB, from fibrinogen. That is, both fibrinopeptides A-, abbreviated as FPA-, and B-released fibrinogen play important roles to form oriented fibrin intermediate fibers. A polymerization site, revealed after the release of FPB, was considered to bind with its complementary site to grow along the direction of the axis of protofibrils. But protofibrils, formed by FPA-released fibrinogen, seem more rapidly to aggregate toward the lateral direction than FPA- and FPB-released fibrinogen. Although clots formed by thrombin and Reptilase have been observed to be very similar in structure, they could be distinguished under flow birefringence observation.
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Sato, H., Mizui, Y. Flow Birefringence in the Polymerization of Fibrinogen Catalyzed by Thrombin and Undetectable in Reptilase Systems under the Corresponding Conditions. Polym J 21, 77–83 (1989). https://doi.org/10.1295/polymj.21.77
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DOI: https://doi.org/10.1295/polymj.21.77