title: Rat liver kininase, a serine peptidase.
abstract: A serine peptidase (RLK1) was partially purified from rat liver homogenates. Its molecular weight was 80,000, and its optimum pH was 7.5. Bz-Tyr-O-Et was hydrolyzed by the enzyme, which was inhibited by Ip2PF, PMSF and by Tos-Phe-CH2Cl. The bonds cleaved by the enzyme were Phe5-Ser6 and Phe8-Arg9, when bradykinin was used as substrate.
mesh_terms: D000818:Animals; D010450:Endopeptidases / Q000302:isolation & purification*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000032:analysis; D011480:Protease Inhibitors / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains; D012697:Serine Endopeptidases
chemical_list: D011480:Protease Inhibitors; D010450:Endopeptidases; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases