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  • Title: The slow-binding inhibition of cathepsin K by its propeptide.
    Author: Billington CJ, Mason P, Magny MC, Mort JS.
    Journal: Biochem Biophys Res Commun; 2000 Oct 05; 276(3):924-9. PubMed ID: 11027570.
    Abstract:
    A peptide corresponding to the full-length proregion (amino acids 16-114) of human cathepsin K was expressed and purified from Escherichia coli. This recombinant propeptide was investigated for its ability to inhibit the activity of three cysteine proteinases: cathepsins K, L, and B. Kinetic studies showed the propeptide to be a potent slow-binding inhibitor of its parent enzyme with a K(i) = 2. 61 nM at pH 6. This inhibition was pH-dependent, with a decrease in pH from 6 to 4 leading to a concomitant increase in K(i) to 147 nM. The propeptide also inhibited cathepsin L with a K(i) = 26.1 nM at pH 6, but showed little inhibition of cathepsin B at concentrations up to 400 nM.
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