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

被引：0
|
作者：
Jack N. Losso
Cate N. Munene
Rishipal R. Bansode
Hiba A. Bawadi
机构：
[1] Louisiana State University Agricultural Center,Food Protein Biotechnology Laboratory, Department of Food Science
来源：
Biotechnology Letters | 2004年 / 26卷
关键词：
angiogenesis; heparin-enhanced zymography; matrix metalloproteinase-1; quenched fluorescence substrate hydrolysis; soybean Bowman–Birk inhibitor;
D O I：
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学科分类号：
摘要：
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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页码：901 / 905
页数：4
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