Specific assay method for the activities of cathepsin L-type cysteine proteinases.
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.
Inubushi
T
T
Institute for Health Sciences, Tokushima Bunri University.
Kakegawa
H
H
Kishino
Y
Y
Katunuma
N
N
D000595:Amino Acid Sequence; D000818:Animals; D056668:Cathepsin L; D002403:Cathepsins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D010450:Endopeptidases; D008297:Male; D008969:Molecular Sequence Data; D051381:Rats; D017208:Rats, Wistar; D013379:Substrate Specificity
D015853:Cysteine Proteinase Inhibitors; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D056668:Cathepsin L; C534280:Ctsl protein, rat