Kirschke H, Wiederanders B, Brömme D, Rinne A
Institute of Biochemistry, Medical Faculty, Martin-Luther University, Halle, Saale, German Democratic Republic.
Biochem J. 1989 Dec 1;264(2):467-73. doi: 10.1042/bj2640467.
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.
通过免疫化学方法在牛肾、脾、淋巴结和肺中检测到组织蛋白酶S。组织蛋白酶S在肾脏中的免疫染色集中于近端小管的细胞，该酶存在于细胞质颗粒中。从牛脾中纯化组织蛋白酶S的方法包括硫酸铵分级分离、CM - 葡聚糖凝胶C - 50柱色谱、Sephacryl S - 200凝胶过滤和色谱聚焦（pH 8.0 - 6.0）。在pH 4.2时，匀浆的自溶作用会使该酶部分失活。组织蛋白酶S的等电点为7.0。发现在pH 7.0以下，组织蛋白酶S水解蛋白质的速率与组织蛋白酶L相似。在pH值为7.0 - 7.5时，组织蛋白酶S保留了大部分活性，而组织蛋白酶L则完全失活。
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