Rigidity moduli of bovine fibrin gels initiated by thrombin¹

Article type: Research Article

Authors: Copley, Alfred L. | King, Robert G. | Scheinthal, Bernard M.

Affiliations: Hemorrhage and Thrombosis Research Laboratories, Veterans Adminstration Hospital, East Orange, N.J. 07019 and Department of Pharmacology, New York Medical College, New York, N.Y. 10029

Note: [1] Aided in part by the Office of Naval Research contracts Nonr 2754(03) and NOOO-14-67-A-4449-0001 with New York Medical College.

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.

DOI: 10.3233/BIR-1970-7201

Journal: Biorheology, vol. 7, no. 2, pp. 81-84, 1970