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Isolation and characterization of a protease inhibitor from commercial stem bromelain acetone powder

✍ Scribed by Perlstein, Seymour H. ;Kéazdy, Ferenc J.

Publisher: Wiley (John Wiley & Sons)
Year: 1973
Tongue: English
Weight: 288 KB
Volume: 1
Category: Article
ISSN: 0091-7419
DOI: 10.1002/jss.400010309

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✦ Synopsis

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 (K~i~ ≈ 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.

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