Inhibition of matrix metalloproteinase-1 activity by the soybean Bowman-Birk inhibitor.
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.
Food Protein Biotechnology Laboratory, Department of Food Science, Louisiana State University Agricultural Center, 111 Food Science Building, Baton Rouge, LA 70803, USA. jlosso@lsu.edu
Jack N
JN
Losso
Cate N
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Munene
Rishipal R
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Bansode
Hiba A
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Bawadi
D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000737:chemistry; D006868:Hydrolysis; D020781:Matrix Metalloproteinase 1 / Q000737:chemistry*; D061965:Matrix Metalloproteinase Inhibitors; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D014358:Trypsin Inhibitor, Bowman-Birk Soybean / Q000737:chemistry*
D004791:Enzyme Inhibitors; D061965:Matrix Metalloproteinase Inhibitors; D014358:Trypsin Inhibitor, Bowman-Birk Soybean; D020781:Matrix Metalloproteinase 1