title: [Inhibitors of cathepsin R (ribosomal proteinase). Polyamines as natural inhibitors of the proteinase].
abstract: The effects of potential inhibitors on the activity of neutral ribosomal proteinase--cathepsis R--were studied. It was found that cathepsin R belongs to the group of serine enzymes. The polyamines spermine and spermidine, which are inherently present in the ribosomes, are natural reversible inhibitors of cathepsin R. Upon separation of the enzyme from the inhibitors the proteinase displays a high activity. The effects of polyamines on the proteinase activity may either be direct or mediated via RNA. The enzyme activity can also be controlled by amino acids. Approximately 2/3 of cathepsis R were found in a latent state.
mesh_terms: D000818:Animals; D002403:Cathepsins / Q000037:antagonists & inhibitors*; D008297:Male; D011073:Polyamines / Q000494:pharmacology*; D051381:Rats; D012270:Ribosomes / Q000201:enzymology; D012694:Serine; D013095:Spermidine / Q000494:pharmacology; D013096:Spermine / Q000494:pharmacology
chemical_list: D011073:Polyamines; D013096:Spermine; D012694:Serine; D002403:Cathepsins; D013095:Spermidine
vernacular_title: Ingibitory katepsina R (proteinazy ribosom) Poliaminy-estestvennye ingibitory proteinazy.