Abstract
Measurements, employing the Weissenberg rheogoniometer, were made of the rigidity modulus of fibrin gels in unidirectional shear. The system of purified preparations of fibrinogen and thrombin was free of transamidase and the fibrin gel was soluble in urea or lithium bromide. Two significant changes were observed in the slope of semilog plot of the rigidity modulus versus time within the first sixty minutes of the conversion of fibrinogen to fibrin. These changes in the slopes are discussed in relation to the roles of fibrinopeptides A and B, as well as other factors which may contribute to the gel structure.
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