Abstract
Activation of plasminogen through surface-mediated reactions is well recognized. In the presence of kaolin, purified Hageman factor (Factor XII) changed plasminogen to plasmin, as assayed upon a synthetic amide substrate and by fibrinolysis. Kinetic studies suggested an enzymatic action of Hageman factor upon its substrate, plasminogen. Hageman factor fragments, at a protein concentration equivalent to whole Hageman factor, activated plasminogen to a lesser extent. These protein preparations were not contaminated with other agents implicated in surface-mediated fibrinolysis. Diisopropyl fluorophosphate treatment of plasminogen did not inhibit its activation by Hageman factor. These studies indicate that Hageman factor has a hitherto unsuspected function, the direct activation of plasminogen.
MeSH Terms
Amides/blood
Factor XII/analogs & derivatives,antagonists & inhibitors,pharmacology
Fibrinolysis
Humans
In Vitro Techniques
Peptide Fragments/pharmacology
Plasminogen Activators
Chemicals
Amides
Peptide Fragments
Factor XII
Plasminogen Activators
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Goldsmith G H
Saito H
Ratnoff O S
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