Abstract
Fibrin is formed via polymerization of one of the main blood proteins, fibrinogen, under the action of an enzyme, thrombin. Dynamic surface elasticity and dynamic surface tension of mixed solutions of fibrinogen and thrombin are measured as functions of surface age and enzyme concentration (50–800 U/L). The nonmonotonic pattern of the dependences for the dynamic surface elasticity indicates the multistage character of fibrin film formation and makes it possible to monitor the transition from unfolded protein to individual filamentous aggregates; a network of branched fibrils; and, finally, a continuous film. The dynamic surface elasticity of fibrin films is twofold higher than the corresponding values for fibrinogen (115 and 55 mN/m, respectively). The use of different types of microscopy makes it possible to assess the morphology of the obtained films.
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