Interaction between duodenase, a proteinase with dual specificity, and soybean inhibitors of Bowman-Birk and Kunitz type

Authors
Gladysheva, IP Zamolodchikova, TS Sokolova, EA Larionova, NI
Citation
Ip. Gladysheva et al., Interaction between duodenase, a proteinase with dual specificity, and soybean inhibitors of Bowman-Birk and Kunitz type, BIOCHEM-MOS, 64(11), 1999, pp. 1244-1249
Citations number
35
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMISTRY-MOSCOW
ISSN journal
00062979 → ACNP
Volume
64
Issue
11
Year of publication
1999
Pages
1244 - 1249
Database
ISI
SICI code
0006-2979(199911)64:11<1244:IBDAPW>2.0.ZU;2-3
Abstract
The interaction between duodenase, which belongs to a group of Janus-faced proteinases, and classical Bowman-Birk (BBI) and Kunitz (STI) type inhibito rs from soybean was investigated. Duodenase was shown to interact only with the antichymotrypsin site (Leu-Ser) of BBI, whereas the antitrypsin site ( Lys-Ser) of the inhibitor appeared to be vacant and capable of interaction with trypsin. The inhibition constants of duodenase by BBI, the BBI-trypsin complex, and STI were 4, 400, and 40 nM, respectively.