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.
D000818:Animals; D001777:Blood Coagulation / Q000187:drug effects; D002417:Cattle; D004305:Dose-Response Relationship, Drug; D005337:Fibrin / Q000378:metabolism; D005340:Fibrinogen / Q000378:metabolism*; D008628:Mercury / Q000494:pharmacology*; D011108:Polymers; D013917:Thrombin / Q000494:pharmacology
D011108:Polymers; D005337:Fibrin; D005340:Fibrinogen; D013917:Thrombin; D008628:Mercury