Cystatin C functions in vitro and in vivo. Studies on target enzyme inhibition by cystatin C variants and cystatin C deficient mice.
Cystatin C variants with Arg8, Leu9 and/or Val10 replaced by Gly residues were produced by site-directed mutagenesis and E. coli expression. Their interactions with the target proteases, cathepsin B, L, H and S, were studied in vitro in order to provide basic structure-function information of use in the design of specific inhibitors for therapeutic use. Val10 was shown to be the most contributing
