The Ribosomal Serine Proteinase, Cathepsin R
- 1 June 1982
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 125 (1) , 21-26
- https://doi.org/10.1111/j.1432-1033.1982.tb06645.x
Abstract
Ribosomes contain a proteolytic activity, characterized as an endopeptidase with serine in the active center. The enzyme was given the name cathepsin R, following the recommendations of Barrett et al. for naming new proteinases. The present paper contains evidence that cathepsin R in rat liver ribosomes is present in a cryptic form. Upon dissociation of ribosomes to subunits (and to minor extent also by 0.5 M KCl washes), the cryptic proteinase is released. Activation of the released cathepsin R is effected by equilibration with 2 M NaCl/0.05 M sodium acetate, pH 4.8. The MW of free cathepsin R is 25,000-30,000.This publication has 16 references indexed in Scilit:
- PROTEOLYTIC EVENTS IN REPLICATION OF ANIMAL VIRUSESAnnals of the New York Academy of Sciences, 1980
- Role of Cellular and Viral Proteases in the Processing of Picornavirus ProteinsPublished by Springer Nature ,1979
- Protease activity associated with HeLa cell ribosomesBiochemical and Biophysical Research Communications, 1977
- Sensitive, solid-phase assay of proteolytic activityAnalytical Biochemistry, 1976
- Biochemie natürlicher Proteinase‐InhibitorenAngewandte Chemie, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Separation of Large Quantities of Ribosomal Subunits by Zonal UltracentrifugationEuropean Journal of Biochemistry, 1970
- Ribosomal ProteinsPublished by Springer Nature ,1969
- Strukturveränderungen und Dissoziation von Leberribosomen in Abhängigkeit von der Mg++ ‐KonzentrationEuropean Journal of Biochemistry, 1968
- PROTEOLYTIC ENZYMESAnnual Review of Biochemistry, 1960