C-terminal lysine residues of fibrinogen fragments essential for binding to plasminogen

Experiments involving affinity chromatography on immobilized plasminogen columns and the concomitant use of plasmin and carboxypeptidase B indicate that the COOH-terminal lysine residues formed by plasmin-catalyzed cleavage of fibrinogen are essential for the high-affinity binding of the resulting cleavage products to plasminogen.