Influence of Hydrostatic Pressure on the Reversible Polymerization of Fibrin Monomers

Abstract

THE conversion of fibrinogen to fibrin, which is the last stage of the complex process of blood coagulation, is composed of three successive reactions¹: an enzymatic hydrolysis by thrombin of four arginyl-lysyl bonds per molecule of fibrinogen, yielding a fibrin monomer; a spontaneous polymerization of monomers to form a gel or fibrin clot; and an enzymatic transamidation by fibrin stabilizing factor (factor XIII or fibrinase) between ε-amino groups of lysyl and glutaminyl side chains. The mechanism of the reversible polymerization of fibrin monomers remains largely unknown, although it can be studied separately because fibrin monomers can be stabilized in acidic media of high ionic strength such as 1 M NaBr, pH 5.3².