Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins

Biochem J. 1989 Dec 1;264(2):467-73. doi: 10.1042/bj2640467.

Abstract

Cathepsin S was detected in bovine kidney, spleen, lymph nodes and lung by immunochemical methods. The immunostaining of cathepsin S in kidney was concentrated to the cells of the proximal tubule, where the enzyme was present in cytoplasmic granules. The purification method for cathepsin S from bovine spleen involved (NH4)2SO4 fractionation, chromatography on CM-Sephadex C-50, gel filtration on Sephacryl S-200 and chromatofocusing (pH 8.0-6.0). The enzyme was partially destroyed by autolysis of the homogenate at pH 4.2. The isoelectric point of cathepsin S was 7.0. Cathepsin S was found to hydrolyse proteins at a similar rate to cathepsin L below pH 7.0. At pH values of 7.0-7.5 cathepsin S retained most of its activity, whereas cathepsin L was completely inactive.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cathepsins / analysis
  • Cathepsins / isolation & purification*
  • Cathepsins / metabolism
  • Cattle
  • Electrophoresis, Polyacrylamide Gel
  • Glycosylation
  • Immune Sera
  • Immunoblotting
  • Immunoenzyme Techniques
  • Isoelectric Focusing
  • Kidney / enzymology*
  • Kidney Cortex / cytology
  • Kidney Cortex / enzymology
  • Kidney Tubules, Proximal / cytology
  • Kidney Tubules, Proximal / enzymology
  • Kinetics
  • Lung / enzymology
  • Lymph Nodes / enzymology
  • Molecular Weight
  • Spleen / cytology
  • Spleen / enzymology*
  • Substrate Specificity

Substances

  • Immune Sera
  • Cathepsins
  • cathepsin S