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- W2144804960 abstract "Seven closely related protease inhibitors were isolated from commercial bromelain acetone powder in electrophoretically pure form by gel filtration on Sephadex G-75, followed by ion exchange chromatography on DEAE Sephadex at pH 7.55. The inhibitors are proteins of MW 5000-6000, which inhibit competitively the bromelaincatalyzed hydrolysis of CLN (Ki ≈ 10−7 M). This inhibition is optimal at pH 3 to 4,. and it depends upon the ionization of two acidic residues of pK = 4.5 and 5.0. In the acidic pH range the inhibitors are also effective toward papain, ficin and trypsin." @default.
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- W2144804960 date "1973-01-01" @default.
- W2144804960 modified "2023-09-26" @default.
- W2144804960 title "Isolation and characterization of a protease inhibitor from commercial stem bromelain acetone powder" @default.
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- W2144804960 doi "https://doi.org/10.1002/jss.400010309" @default.
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