The action of bovine spleen cathepsins B and D on the cytoplasmic ribonuclease inhibitor from rat liver.
The inactivation by the lysosomal cathepsins B or D of the cytoplasmic neutral ribonuclease inhibitor has been investigated with respect to the required amounts of cathepsin, optimal pH and time course. With a pH optimum between 5 and 5.5, a possible role of these endopeptidases in regulating the inhibitor and, concomitantly, the ribonuclease and RNA concentrations in the cell is discussed.
D000818:Animals; D002352:Carrier Proteins; D002401:Cathepsin B; D002402:Cathepsin D; D002403:Cathepsins / Q000494:pharmacology*; D003593:Cytoplasm / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D010179:Pancreas / Q000201:enzymology; D011506:Proteins / Q000037:antagonists & inhibitors*; D051381:Rats; D012260:Ribonucleases / Q000037:antagonists & inhibitors*; D013154:Spleen / Q000201:enzymology*
D002352:Carrier Proteins; D011506:Proteins; C028666:Rnh1 protein, rat; D012260:Ribonucleases; D002403:Cathepsins; D002401:Cathepsin B; D002402:Cathepsin D