Abstract
Summary
Equilibration of human plasmin-streptokinase mixtures at pH 2 led to a loss in ability of mixture to convert bovine plasminogen to plasmin. Plasminogen conversion activity could be re-established upon readdition of streptokinase. Results of repeated low pH treatments and readditions of streptokinase do not seem to support the hypothesis of the existence of a specific proactivator for formation of a singular plasminogen activator. Studies on the influence of a plasmin inhibitor, added at various stages of the interactions, on formation of plasminogen converting activity yielded results in agreement with the hypothesis that plasmin reacts, probably proportionally, with streptokinase to form a plasmin-streptokinase complex which has the ability to convert bovine plasminogen to plasmin.
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