Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins. |
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Authors: | H Kirschke B Wiederanders D Br?mme A Rinne |
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Affiliation: | Institute of Biochemistry, Medical Faculty, Martin-Luther University, Halle, Saale, German Democratic Republic. |
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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. |
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