title: [Kininogenase activity of cathepsins D].
abstract: The kininogenase activity of highly purified preparations of cathepsins D from human liver and spleen, leukemic infiltrate obtained from patients with myeloic leukemia, and from chicken liver was studied. It was found that pepstatin, a specific inhibitor of carboxylic proteinases, inhibits this activity of cathepsins D. Interaction of chicken liver cathepsin D with human plasma substrate, which is possibly a low molecular weight kininogen (Ks = 1.3.10(-7) M) results in a production of the bradikinin analog methionyl-lysyl-bradikinin. The role of cathepsins D as potent inflammatory agents responsible for the generation of biologically active peptides--mediators of inflammation from the protein substrates including kininogens under desintegration of lysosomes is discussed.
mesh_terms: D000818:Animals; D002402:Cathepsin D; D002403:Cathepsins / Q000378:metabolism*; D002645:Chickens; D006801:Humans; D007610:Kallikreins / Q000378:metabolism*; D007700:Kinetics; D007704:Kininogens; D007951:Leukemia, Myeloid / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D008970:Molecular Weight; D010436:Pepstatins / Q000494:pharmacology; D013154:Spleen / Q000201:enzymology
chemical_list: D007704:Kininogens; D010436:Pepstatins; D002403:Cathepsins; D007610:Kallikreins; D002402:Cathepsin D
vernacular_title: Kininogenaznaia aktivnost' katepsinov D.