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

Jack N Losso; Cate N Munene; Rishipal R Bansode; Hiba A Bawadi

doi:10.1023/b:bile.0000025900.33812.7c

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

Biotechnol Lett. 2004 Jun;26(11):901-5. doi: 10.1023/b:bile.0000025900.33812.7c.

Authors

Jack N Losso¹, Cate N Munene, Rishipal R Bansode, Hiba A Bawadi

Affiliation

¹ 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

PMID: 15269538
DOI: 10.1023/b:bile.0000025900.33812.7c

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 types

Research Support, Non-U.S. Gov't

MeSH terms

Enzyme Activation
Enzyme Inhibitors / chemistry
Hydrolysis
Matrix Metalloproteinase 1 / chemistry*
Matrix Metalloproteinase Inhibitors
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods*
Trypsin Inhibitor, Bowman-Birk Soybean / chemistry*

Substances

Enzyme Inhibitors
Matrix Metalloproteinase Inhibitors
Trypsin Inhibitor, Bowman-Birk Soybean
Matrix Metalloproteinase 1