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  • Journal
    Digital Access
    Provider
    Version
    CINAHL
    v. 1-14, 1999-2012.
    Acad Search Prem
    v. 1-14, 1999-2012.
    TandFonline
    v. 1-13, 1999-2011.
  • Article
    Menegatti E, Ferroni R, Benassi CA, Rocchi R.
    Int J Pept Protein Res. 1977;10(2):146-52.
    Arginine residues (5.5 out of 6) of the trypsin-kallikrein inhibitor from bovine organs (Kunitz inhibitor) were selectively modified by reaction with 1, 2-cyclohexanedione in sodium borate buffer, pH 9.0. The modified inhibitor is still highly active in inhibiting trypsin and chymotrypsin at 1:1 inhibitor: enzyme molar ratio and full inhibition was achieved at slightly higher molar ratio. The extent of correct refolding, upon reoxidation, of the reduced, arginine-modified inhibitor is diminished and regeneration of two arginines occurred under the reduction conditions. The stability constants and the standard-free energies of binding of the complexes between trypsin, or chymotrypsin, and the native, the arginine-modified and the reduced and reoxidized arginine-modified inhibitor have been determined from inhibitory assays.
    Digital Access Access Options