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Title: Interaction between duodenase, a proteinase with dual specificity, and soybean inhibitors of Bowman-Birk and Kunitz type. Author: Gladysheva IP, Zamolodchikova TS, Sokolova EA, Larionova NI. Journal: Biochemistry (Mosc); 1999 Nov; 64(11):1244-9. PubMed ID: 10611528. Abstract: The interaction between duodenase, which belongs to a group of Janus-faced proteinases, and classical Bowman--Birk (BBI) and Kunitz (STI) type inhibitors 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.[Abstract] [Full Text] [Related] [New Search]