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• W273708051 abstract "ABSTRACT Human liver contains cathepsins B, H and L, like rat liver. Cathepsin B has high activity against synthetic substrates containing di-arginine, which suggests that it may contribute to the cleavage of bonds at “di-basic” sequences that is important in the processing of many precursor proteins. It can also show a quite different activity, however, cleaving dipeptides sequentially from the C-terminus of a polypeptide chain. Cathepsin H is an endopeptidase which also has a broad aminopeptidase activity; it differs from cathepsin B in other aspects of specificity, and in sensitivity to inhibitors. Cathepsin L is a powerful endopeptidase with little or no action on the usual synthetic substrates of cathepsins B and H; it is very active against collagen, and may be identical with “c ollagenolytic cathepsin ”." @default.
• W273708051 created "2016-06-24" @default.
• W273708051 creator A5032943700 @default.
• W273708051 date "1980-01-01" @default.
• W273708051 modified "2023-10-17" @default.
• W273708051 title "THIOL PROTEINASES OF HUMAN LYSOSOMES" @default.
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• W273708051 doi "https://doi.org/10.1016/b978-0-08-024417-4.50032-9" @default.
• W273708051 hasPublicationYear "1980" @default.
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