Interaction between Duodenase, a Proteinase with Dual Specificity, and Soybean Inhibitors of Bowman-Birk and Kunitz Type

I. P. Gladysheva, T. S. Zamolodchikova, E. A. Sokolova, N. I. Larionova

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1244-1249
Number of pages6
JournalBiochemistry (Moscow)
Volume64
Issue number11
StatePublished - Nov 1999
Externally publishedYes

Keywords

  • Bowman-birk inhibitor
  • Duodenase
  • Inhibition constant
  • Kunitz inhibitor
  • Specificity

ASJC Scopus subject areas

  • Biochemistry

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