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Dissimilarity of human vascular plasminogen activator and human urokinase.

Abstract A plasminogen activator extracted from the vascular tree of human cadavers was examined for its relationship to human urokinase. The vascular activator was found to be different from urokinase in terms of immunologic reaction, enzymatic activity, and molecular weight. Gammaglobulins prepared from specific antisera to human urokinase did not inhibit the activity of the vascular activator, whereas they strongly inhibited the urokinase activity. Kinetic analysis of the hydrolysis of the synthetic substrate, acetyl lysin methyl ester, by both enzymes revealed that these hydrolyze the substrate at dissimilar rates with different K M values. The molecular weight of the vascular activator was estimated to be approximately 65,000 by gel filtration, while a value of 55,000 was obtained for urokinase. The vascular activator was inhibited by the urokinase inhibitor from the placenta, but to a lesser degree than the urokinase was inhibited under the same conditions.