Interaction of fibrinogen with mercury

The interaction of bovine fibrinogen with mercuric chloride was studied. Gel filtration on Sephadex G-25 revealed that fibrinogen bound twice the amount of mercury such as fibrin or fibrin monomers (8.8, 4.5, and 3.4 micrograms Hg2+ ions/mg protein, respectively). Fibrinogen complexed with mercury or in the presence of Hg2+ ions at concentration above 10-6 M was clotted by thrombin more effectively than in the control system which was devoid of this metal. Reaggregation of the purified fibrin monomers was not affected by mercury.