Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins.
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.
Kirschke
H
H
Institute of Biochemistry, Medical Faculty, Martin-Luther University, Halle, Saale, German Democratic Republic.
Wiederanders
B
B
Brömme
D
D
Rinne
A
A
D000818:Animals; D002403:Cathepsins / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D007106:Immune Sera; D015151:Immunoblotting; D007124:Immunoenzyme Techniques; D007525:Isoelectric Focusing; D007668:Kidney / Q000201:enzymology*; D007672:Kidney Cortex / Q000166:cytology / Q000201:enzymology; D007687:Kidney Tubules, Proximal / Q000166:cytology / Q000201:enzymology; D007700:Kinetics; D008168:Lung / Q000201:enzymology; D008198:Lymph Nodes / Q000201:enzymology; D008970:Molecular Weight; D013154:Spleen / Q000166:cytology / Q000201:enzymology*; D013379:Substrate Specificity
D007106:Immune Sera; D002403:Cathepsins; C028217:cathepsin S