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.
Losso
Jack N
JN
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
Munene
Cate N
CN
Bansode
Rishipal R
RR
Bawadi
Hiba A
HA
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