The Influence of the End Products of Plasmin-Mediated Hydrolysis of Fibrinogen and Fibrin (E F and E f Fragments) on Fibrinogen Cross-linking

We studied the influence of the end products of plasmin-mediated hydrolysis of fibrinogen and nonstabilized fibrin (E_F and E_f fragments) on covalent cross-linking of fibrinogen molecules catalyzed by a fibrin-stabilizing factor (factor XIIIa). The data on elastic and dynamic light scattering reveal no difference in the spatial structure of covalently linked fibrinogen molecules in the presence of the hydrolysis end products E_F and E_f. In contrast to the inactive fragment E_F, fragment E_f significantly accelerates the enzymatic reaction. This is also confirmed by electrophoresis of the reduced samples indicating a relatively fast accumulation of -dimers and A-polymers as compared to the control samples. Possible molecular mechanisms of this effect are discussed.