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.
Christensen
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D002846:Chromatography, Affinity; D005340:Fibrinogen / Q000032:analysis*; D005341:Fibrinolysin / Q000378:metabolism; D006801:Humans; D007122:Immunoelectrophoresis; D008239:Lysine / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D010958:Plasminogen / Q000378:metabolism*
D010446:Peptide Fragments; D005340:Fibrinogen; D010958:Plasminogen; D005341:Fibrinolysin; D008239:Lysine