Study on interaction between duodenase   protease with dual specificity and inhibitors of bowman-birk family.
The interaction between duodenase and inhibitors of Bowman-Birk type from soybeans (BBI) and lima beans (LBI) was investigated. Duodenase was shown to interact only with antichymotrypsin site of these inhibitors. The inhibition constants of duodenase by BBI, LBI, BBI-trypsin and LBI trypsin complexes were 4, 23, 400, 600 (n)M respectively.
Department of Chemical Enzymology, School of Chemistry, Lomonosov Moscow State University, Moscow, 119899 Russia.
Inna P Gladysheva
IP
Gladysheva
Natalia A
NA
Popykina
Tatyana S
TS
Zamolodchikova
Natalia I
NI
Larionova
D001665:Binding Sites; D004305:Dose-Response Relationship, Drug; D007700:Kinetics; D027805:Phaseolus / Q000378:metabolism; D010940:Plant Proteins / Q000737:chemistry*; D011485:Protein Binding; D012697:Serine Endopeptidases / Q000737:chemistry*; D013379:Substrate Specificity; D013997:Time Factors; D014358:Trypsin Inhibitor, Bowman-Birk Soybean / Q000737:chemistry*; D000514:alpha 1-Antichymotrypsin / Q000737:chemistry
D010940:Plant Proteins; D014358:Trypsin Inhibitor, Bowman-Birk Soybean; D000514:alpha 1-Antichymotrypsin; C025398:protease inhibitor protein, Phaseolus lunatus; D012697:Serine Endopeptidases; C078261:duodenase