Activation of prokallikrein in the rat kidney by proteases.
Prokallikrein was activated by trypsin and by alpha-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 micrograms to 1 mg per ml in PBS and that by alpha-chymotrypsin was at the concentration of 5 mg per ml. The enzymic properties of trypsin-activated and alpha-chymotrypsin-activated kallikreins were identical with those of active kallikrein in the kidney.
D000818:Animals; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002918:Chymotrypsin / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D007610:Kallikreins / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology*; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000494:pharmacology*; D011288:Prekallikrein / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D014357:Trypsin / Q000494:pharmacology
D011288:Prekallikrein; D010447:Peptide Hydrolases; D007610:Kallikreins; D002918:Chymotrypsin; D014357:Trypsin