T-kinin is released from T-kininogen by consecutive cleavage by cathepsin E-like proteinase and 72 kDa proteinase.
Using highly purified T-kininogen and cathepsin E-like proteinase and 72 kDa proteinase in rat spleen, the release of T-kinin from T-kininogen was found to occur by consecutive cleavage by cathepsin E-like proteinase and 72 kDa proteinase. 72 kDa proteinase seems to be serine proteinase, because it was completely inhibited by diisopropyl fluorophosphate but not by pepstatin, leupeptin and bestatin.
D000818:Animals; D001920:Bradykinin / Q000031:analogs & derivatives* / Q000378:metabolism; D020059:Cathepsin E; D002403:Cathepsins / Q000378:metabolism*; D007700:Kinetics; D007704:Kininogens / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D013154:Spleen / Q000201:enzymology*
D007704:Kininogens; C039065:T-kinin; D002403:Cathepsins; D010447:Peptide Hydrolases; D020059:Cathepsin E; D001920:Bradykinin