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    Biochem Biophys Res Commun. 1990 Mar 16;167(2):716-21.

    Protease-specificity of Kunitz inhibitor domain of Alzheimer's disease amyloid protein precursor.

    Kido H, Fukutomi A, Schilling J, Wang Y, Cordell B, Katunuma N.

    Source

    Division of Enzyme Chemistry, University of Tokushima, Japan.

    Abstract

    The putative inhibitor domain of Alzheimer's disease amyloid protein precursor was purified from E. coli containing a synthetic gene encoding the Kunitz domain. The purified protein (A4 inhibitor) inhibited the activity of trypsin, forming a 1:1 molar complex with the enzyme. It also strongly inhibited plasmin (Ki = 7.5 x 10(-11) M) from human serum and tryptase (Ki = 2.2 x 10(-10) M) from rat mast cells (tryptase M). In addition, it inhibited rat pancreatic trypsin, alpha-chymotrypsin and kallikrein and human serum kallikrein, but did not inhibit rat chymase, pancreatic elastase, alpha-thrombin, urokinase, papain or cathepsin B.

    PMID:
    1969731
    [PubMed - indexed for MEDLINE]

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