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组织蛋白酶L型半胱氨酸蛋白酶活性的特异性检测方法。

Specific assay method for the activities of cathepsin L-type cysteine proteinases.

作者信息

Inubushi T, Kakegawa H, Kishino Y, Katunuma N

机构信息

Institute for Health Sciences, Tokushima Bunri University.

出版信息

J Biochem. 1994 Aug;116(2):282-4. doi: 10.1093/oxfordjournals.jbchem.a124520.

DOI:10.1093/oxfordjournals.jbchem.a124520
PMID:7822244
Abstract

We have established a new differential assay method for cathepsin L-type proteinases using specific inhibitors, E-64 for all cysteine proteinases, CA-074 for cathepsin B, and PLCPI for cathepsin L-type proteinases with Z-Phe-Arg-MCA as the substrate. The value of cathepsin B calculated by this method did not coincide with value assayed directly in terms of the hydrolysis of Z-Arg-Arg-MCA, a specific substrate for cathepsin B. The activities of cathepsin L-type proteinases, cathepsins B and J in rat liver and kidney were assayed at the same time using this new assay method as a representative example.

摘要

我们建立了一种新的组织蛋白酶L型蛋白酶的差异检测方法,该方法使用特异性抑制剂,即针对所有半胱氨酸蛋白酶的E-64、针对组织蛋白酶B的CA-074以及针对组织蛋白酶L型蛋白酶的PLCPI,并以Z-Phe-Arg-MCA作为底物。通过该方法计算得到的组织蛋白酶B的值,与使用组织蛋白酶B的特异性底物Z-Arg-Arg-MCA直接检测得到的值不一致。以这种新的检测方法为代表,同时检测了大鼠肝脏和肾脏中组织蛋白酶L型蛋白酶、组织蛋白酶B和组织蛋白酶J的活性。

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