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. 1990 Mar 16;167(2):716-21.
doi: 10.1016/0006-291x(90)92084-d.

Protease-specificity of Kunitz Inhibitor Domain of Alzheimer's Disease Amyloid Protein Precursor

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Protease-specificity of Kunitz Inhibitor Domain of Alzheimer's Disease Amyloid Protein Precursor

H Kido et al. Biochem Biophys Res Commun. .

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.

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