Fibrin monomer was prepared from purified human fibrinogen by the action of insolubilized
thrombin in the presence of 3.3 M urea. As judged by N-terminal amino acid analyses,
complete conversion of fibrinogen to fibrin was achieved. The preparation proved homogeneous
by gel chromatography and SDS electrophoresis and had retained clotting abilities
identical to those of fibrin monomers arising from fibrinogen exposed to large amounts
of thrombin. No changes were observed after freezing in liquid nitrogen or after storage
at +4°C for 4 weeks. As to homogeneity and ability to polymerize the preparation proved
superior to those fibrin monomer preparations obtained by dissolution of polymerized
fibrin in various solvents.
