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- W2000755055 abstract "Cystatin C with the 11 N‐terminal amino acids truncated shows a much lower affinity for cysteine proteinases than the intact inhibitor. Such truncation of cystatin C is recorded after action of glycyl endopeptidase and cathepsin L. Incubation of cystatin C with papain, cathepsin B or cathepsin H led to no changes in the cystatin C molecule. Isoelectric focusing of the cathepsin L and cystatin C mixture showed the formation of two new bands. One of them appeared whether E‐64 or PMSF was added or not, evidently representing a cystatin C/cathepsin L complex. The other band is the truncated cystatin C molecule. N‐terminal sequencing after separation by HPLC showed that cystatin C is cleaved by cathepsin L at the Gly11‐Gly12 bond. The action of cathepsin L on cystatin C may be explained by the cleavage of the scissile bond in an inappropriate complex." @default.
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- W2000755055 date "1999-07-15" @default.
- W2000755055 modified "2023-10-18" @default.
- W2000755055 title "Cathepsin L is capable of truncating cystatin C of 11 N-terminal amino acids" @default.
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- W2000755055 doi "https://doi.org/10.1016/s0014-5793(99)00824-8" @default.
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