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Inhibition of matrix metalloproteinase-1 activity by the soybean Bowman–Birk inhibitor

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Abstract

Inductively coupled plasma analysis of soybean Bowman–Birk inhibitor (BBI) indicated that BBI was a metalloprotein which contained magnesium, calcium, and zinc at 0.40, 0.43 and 0.008 atom/mol BBI, respectively. Heparin-enhanced gelatin zymography, quenched fluorescence substrate hydrolysis analysis, and the Biotrak assay of the interaction of BBI with the matrix metalloproteinase-1 (MMP-1) demonstrated that demineralized BBI at 30 nm inhibited MMP-1 activity whereas mineralized BBI was inhibitory at 115 nm.

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Authors and Affiliations

  1. Food Protein Biotechnology Laboratory, Department of Food Science, Louisiana State University Agricultural Center, 111 Food Science Building, Baton Rouge, LA , 70803, USA

    Jack N. Losso, Cate N. Munene, Rishipal R. Bansode & Hiba A. Bawadi

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  1. Jack N. Losso
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  2. Cate N. Munene
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  3. Rishipal R. Bansode
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  4. Hiba A. Bawadi
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Losso, J.N., Munene, C.N., Bansode, R.R. et al. Inhibition of matrix metalloproteinase-1 activity by the soybean Bowman–Birk inhibitor. Biotechnology Letters 26, 901–905 (2004). https://doi.org/10.1023/B:bile.0000025900.33812.7c

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  • DOI: https://doi.org/10.1023/B:bile.0000025900.33812.7c

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