Inhibition of matrix metalloproteinase-1 activity by the soybean Bowman-Birk inhibitor
Document Type
Article
Publication Date
6-1-2004
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.
Publication Source (Journal or Book title)
Biotechnology Letters
First Page
901
Last Page
905
Recommended Citation
Losso, J., Munene, C., Bansode, R., & Bawadi, H. (2004). Inhibition of matrix metalloproteinase-1 activity by the soybean Bowman-Birk inhibitor. Biotechnology Letters, 26 (11), 901-905. https://doi.org/10.1023/B:bile.0000025900.33812.7c