Thromb Haemost 1979; 41(02): 357-364
DOI: 10.1055/s-0038-1646785
Original Articles
Schattauer GmbH Stuttgart

The Binding of Diiodosalicylate and Flufenamate to the Plasma Antiactivator: Analysis of Chemical Fibrinolysis

L B Nanninga
The Department of Physiology and Biophysics, University of Texas Medical Branch, Galveston, Texas 77550
› Author Affiliations
Further Information

Publication History

Received 21 January 1978

Accepted 10 April 1978

Publication Date:
09 July 2018 (online)

Summary

The fibrinolytic effect of diiodosalicylate was expressed as apparent units urokinase. The dissociation constant of the urokinase-inhibitor complex is increased 19 times in the presence of 10-2 M diiodosalicylate. The binding of diiodosalicylate to the antiactivator was estimated and the increase in free urokinase in the presence of diiodosalicylate was calculated. With 10-2 M diiodosalicylate present only 4% of the inhibitor remains free to bind urokinase. Therefore, the fibrinolytic action of diiodosalicylate can be explained on the basis of its binding to the inhibitor and the release of free urokinase.

 
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