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.