Abstract
In prepns. of bovine plasminogen, streptokinase (SK) produced plasmin activities much smaller than those caused by other activators. Human globulin added to SK and bovine plasminogen produced activities much larger than the sum of the controls (SK + human globulin; SK + bovine plasminogen). In human globulin SK forms a large excess of plasminogen activator, which produces high activities in bovine plasminogen. Hence SK transforms a proactivator in blood to an activator, which converts plasminogen to plasmin. A low content of proactivator in bovine blood is the cause of the incomplete activation of prepns. of bovine plasminogen by SK. Casein and plasminogen-free fibrin were used as substrates. Results obtained with normal fibrinolytic methods are difficult to evaluate because of the proactivator and plasminogen contained in the substrate.

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