Abstract
The kinin-forming proteases in human serum were studied. Two serum kallikreins, i.e. enzymes acting directly and specifically on kinin-yielding globulin (kininogen), were separated by ion-exchange chromatography. They were differentiated from plasmin by their high ratio kinin-forming/esterolytic activity, by the absence of fibrinolytic activity, and by a lower Michaelis-Menten constant for the hydrolysis of an arginine ester. Their relationship to enzymes which induce kinin formation mainly by activating serum prekallikreins, was studied.
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