ACTIVATION OF PROKALLIKREIN IN THE RAT KIDNEY BY PROTEASES

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Prokallikrein was activated by trypsin and by α-chymotrypsin, but not by proteases, such as plasmin, thrombin, urokinase, carboxypeptidase B, papain, elastase, pepsin, and cathepsin D. Moreover, rat fresh serum did not activate prokallikrein. Maximum activation of prokallikrein by trypsin was obtained at the concentration of 10 μg to 1 mg per ml in PBS and that by α-chymotrypsin was at the concentration of 5 mg per ml. The enzymic properties of trypsin-activated and α-chymotrypsin-activated kallikreins were identical with those of active kallikrein in the kidney.