Inhibition of matrix metalloproteinase-1 activity by the soybean Bowman-Birk inhibitor.
作者信息
Losso Jack N, Munene Cate N, Bansode Rishipal R, Bawadi Hiba A
机构信息
Food Protein Biotechnology Laboratory, Department of Food Science, Louisiana State University Agricultural Center, 111 Food Science Building, Baton Rouge, LA 70803, USA.
出版信息
Biotechnol Lett. 2004 Jun;26(11):901-5. doi: 10.1023/b:bile.0000025900.33812.7c.
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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