Thromb Haemost 1989; 62(04): 1078-1082
DOI: 10.1055/s-0038-1647121
Original Article
Fibrinolysis
Schattauer GmbH Stuttgart

Plasminogen Interactions with Immobilized Fibrinogen

Burt Adelman
The Department of Medicine and Division of Hematology/Oncology, Medical College of Virginia and Hunter Holmes McGuire Veterans Administration Hospital, Richmond, Virginia, USA
,
Patricia Ouynn
The Department of Medicine and Division of Hematology/Oncology, Medical College of Virginia and Hunter Holmes McGuire Veterans Administration Hospital, Richmond, Virginia, USA
› Author Affiliations
Further Information

Publication History

Received 30 March 1989

Accepted after revision 12 September 1989

Publication Date:
24 July 2018 (online)

Summary

This report describes the binding of plasminogen to fibrinogen adsorbed onto polystyrene wells. Binding was determined by enzyme linked immunosorbent assay. Both glu- and lys-plasminogen bound to immobilized fibrinogen in a dose-dependent fashion. However, more lys- than glu-plasminogen bound when equal concentrations of either were added to immobilized fibrinogen. Plasminogen binding was inhibited by epsilon aminocaproic acid indicating that binding was mediated via lysine-binding regions of plasminogen. Soluble fibrinogen added in excess of immobilized fibrinogen did not compete for plasminogen binding but fibrinogen fragments produced by plasmin digestion of fibrinogen did. Treatment of immobilized fibrinogen with thrombin caused a small but significant (p <0.01) increase in plasminogen binding. These studies demonstrate that immobilized fibrinogen binds both glu- and lys-plasminogen and that binding is mediated via lysine-binding regions. These interactions may facilitate plasminogen binding to fibrinogen adsorbed on to surfaces and to cells such as platelets which bind fibrinogen.

 
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