The inhibitory effect of protamine on the fibrinogenolytic and fibrinolytic activities of plasmin, trypsin and Chymotrypsin A was studied. While the clot fibrinolysis was inhibited by protamine in the presence of the three enzymes, a marked inhibition of the proteolysis of fibrinogen and fibrin was observed only in the presence of Chymotrypsin, a lesser degree of inhibition being observed when plasmin and trypsin were used. The fibrinolysis-inhibiting effect of protamine is brought about by the formation of fibrin-protamine complexes and changes in the clot structure. The structural changes of fibrinogen and fibrin are responsible for their inhibited proteolysis. In the unpurified systems, protamine inhibits fibrinolysis only when the plasma is highly diluted. In the undiluted plasma, quite opposite effects of protamine were observed - that is, fibrinolysis activation probably brought about by the neutralization of plasma antiplasmins by protamine.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.