Study on interaction between duodenase protease with dual specificity and inhibitors of bowman-birk family

Inna P Gladysheva Gladysheva; Natalia A Popykina; Tatyana S Zamolodchikova; Natalia I Larionova

doi:10.2174/0929866023408878

Study on interaction between duodenase protease with dual specificity and inhibitors of bowman-birk family

Protein Pept Lett. 2002 Apr;9(2):139-44. doi: 10.2174/0929866023408878.

Authors

Inna P Gladysheva Gladysheva¹, Natalia A Popykina, Tatyana S Zamolodchikova, Natalia I Larionova

Affiliation

¹ Department of Chemical Enzymology, School of Chemistry, Lomonosov Moscow State University, Moscow, 119899 Russia.

PMID: 12141911
DOI: 10.2174/0929866023408878

Abstract

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.

Publication types

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

MeSH terms

Binding Sites
Dose-Response Relationship, Drug
Kinetics
Phaseolus / metabolism
Plant Proteins / chemistry*
Protein Binding
Serine Endopeptidases / chemistry*
Substrate Specificity
Time Factors
Trypsin Inhibitor, Bowman-Birk Soybean / chemistry*
alpha 1-Antichymotrypsin / chemistry

Substances

Plant Proteins
Trypsin Inhibitor, Bowman-Birk Soybean
alpha 1-Antichymotrypsin
protease inhibitor protein, Phaseolus lunatus
Serine Endopeptidases
duodenase