Summary
The differentiation between plasminogen activators from tissue and urine by means
of the patterns of inhibition produced by epsilon-aminocaproic acid (EACA) in fibrin
plate assays was investigated. Different inhibition patterns reflected genuine differences
between two types of activators. The method allows the differentiation between two
types of activators in weakly fibrinolytic and impure activator solutions.
A biphasic pattern of inhibition by EACA was observed with human urine as well as
with the purified urokinase preparations. The degree of enhancement of fibrinolysis
observed in the millimolar concentration range of EACA fluctuated with the fibrin
substrate and was, in part, related to its plasminogen content. Increasing concentrations
of EACA produced a uniformly increasing inhibition of preparations of tissue activator
obtained in various degrees of purity from porcine ovary and heart. Plasmin was uniformly
inhibited by EACA. Inhibition of plasmin required about 100 times higher concentrations
of EACA than inhibition of tissue activator-induced fibrinolysis. EACA produced a
slightly biphasic pattern of inhibition with plasminogen activator from human uterine
tissue.