Literature DB >> 7106122

The ribosomal serine proteinase, cathepsin R. Occurrence in rat-liver ribosomes in a cryptic form.

J Langner, H Kirschke, P Bohley, B Wiederanders, B D Korant.   

Abstract

Ribosomes have been shown to contain a proteolytic activity, characterized as an endopeptidase with serine in the active center. The enzyme has been given the name cathepsin R, following the recommendations of Barrett et al. (in a publication from the Cold Spring Harbor Laboratory, New York) 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 KC1 washes), the cryptic proteinase is released. Activation of the released cathepsin R is effected by equilibration with 2 M NaC1/0.05 M sodium acetate, pH 4.8. The molecular weight of free cathepsin R is 25 000-30 000.

Entities:  

Mesh:

Substances:

Year:  1982        PMID: 7106122     DOI: 10.1111/j.1432-1033.1982.tb06645.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  3 in total

Review 1.  Proteases and proteolysis in the lysosome.

Authors:  P Bohley; P O Seglen
Journal:  Experientia       Date:  1992-02-15

2.  Purification and partial characterization of poliovirus protease 2A by means of a functional assay.

Authors:  H König; B Rosenwirth
Journal:  J Virol       Date:  1988-04       Impact factor: 5.103

3.  Amino acid control of autophagic sequestration and protein degradation in isolated rat hepatocytes.

Authors:  P O Seglen; P B Gordon
Journal:  J Cell Biol       Date:  1984-08       Impact factor: 10.539

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.