[Inhibition of kininogenase activity of cathepsins D by acid-resistant proteinase inhibitor from rabbit serum].
The inhibitory effect of thermo- and acid-resistant inhibitor of trypsin, chymotrypsin and leukocyte proteinases (TASPI) from rabbit serum on the kininogenase activity of cathepsins D from different organs and tissues (human spleen and liver, chicken liver, spleen leukemic infiltrate from patients with myeloid leukemia) was revealed. The progressive mechanism of TASPI and cathepsins D complexation dependent on time and temperature was revealed. The rate constant of inhibition (ki) of chicken liver cathepsin D by TASPI at 37 degrees was 4,25.10(3)M-1 min-1. It was shown that the kininogenase activity of chicken liver cathepsin D was slightly inhibited by the basic pancreatic trypsin and kallikrein inhibitor from bovine organs (Kunitz type) and by soya bean trypsin inhibitor. The role of TASPI as regulator of cathepsins D activity under pathological conditions accompanied by lysosomal disintegration is discussed.
D000818:Animals; D002402:Cathepsin D; D002403:Cathepsins / Q000037:antagonists & inhibitors*; D007610:Kallikreins / Q000037:antagonists & inhibitors*; D007700:Kinetics; D011480:Protease Inhibitors / Q000097:blood* / Q000494:pharmacology; D011817:Rabbits
D011480:Protease Inhibitors; D002403:Cathepsins; D007610:Kallikreins; D002402:Cathepsin D
Ingibirovanie kininogenaznoĩ aktivnosti katepsinov D kislostabil'nym ingibitorom proteinaz iz syvoretki krovi krolika.