Soybean Bowman-Birk inhibitor conjugates with clinical dextran. Synthesis and antiproteolytic activity

I. P. Gladysheva, N. A. Moroz, A. I. Papisova, N. I. Larionova

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


Conjugates of the classical soybean Bowman-Birk inhibitor (BBI) with clinical dextran were synthesized. Clinical dextran was preliminarily oxidized with periodate to dialdehydedextran (DAD). The effect of the degree of oxidation of DAD on coupling of the inhibitor was evaluated. The binding of the protein was shown to increase with increasing degree of DAD oxidation (5, 10, 20%). Total coupling of the inhibitor occurred when the degree of oxidation of the dextran was 20%. The BBI-DAD (20%) conjugate contained 13% protein with BBI/DAD molar ratio 1 : 1. The conjugates retained the ability to inhibit trypsin (Ki = 0.2-0.3 nM) and alpha-chymotrypsin (Ki = 15-30 nM). Thus, the coupling of BBI with the polymeric carrier caused practically no decrease in the antiproteolytic activity of the inhibitor.

Original languageEnglish (US)
Pages (from-to)474-480
Number of pages7
Issue number4
StatePublished - 2001
Externally publishedYes


  • Bowman-Birk inhibitor
  • Conjugate
  • Dextran

ASJC Scopus subject areas

  • General Chemistry

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