Abstract
1. A plasminogen activator was demonstrated in mammalian bile by the unheated calcium-rich fibrin plate and heated fibrin plate tests.
2. Active fraction, which was free of bile salts, was obtained from bile after gel filtration using Sephadex G-75. Some enzymatic activities of this fraction, which we termed bilokinase (BK), were studied using fibrin, casein and TAMe as substrates.
3. Our results suggest that bilokinase itself is a protease capable of caseinolysis, but only slight fibrinolysis and no TAMe hydrolysis. The activating activity of bilokinase is demonstrable by fibrinolysis and caseinolysis, but not by TAMe hydrolysis. Such activating activity is inhibited by trans-AMCHA, and easily inactivated by heating or pH manipulation.
