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. 1989 Dec 1;264(2):467–473. doi: 10.1042/bj2640467

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

H Kirschke 1, B Wiederanders 1, D Brömme 1, A Rinne 1
PMCID: PMC1133603  PMID: 2690828

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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