Journal article
Soybean Bowman–Birk Inhibitor Conjugates with Clinical Dextran. Synthesis and Antiproteolytic Activity
Biochemistry (Moscow), Vol.66(4), pp.384-389
04/2001
Handle:
https://hdl.handle.net/2376/104869
PMID: 11403644
Abstract
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 (K
i = 0.2-0.3 nM) and α-chymotrypsin (K
i = 15-30 nM). Thus, the coupling of BBI with the polymeric carrier caused practically no decrease in the antiproteolytic activity of the inhibitor.
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Details
- Title
- Soybean Bowman–Birk Inhibitor Conjugates with Clinical Dextran. Synthesis and Antiproteolytic Activity
- Creators
- I Gladysheva - Department of Chemical Enzymology, School of Chemistry Lomonosov Moscow State University Moscow 119899 RussiaN Moroz - Department of Chemical Enzymology, School of Chemistry Lomonosov Moscow State University Moscow 119899 RussiaA Papisova - Department of Chemical Enzymology, School of Chemistry Lomonosov Moscow State University Moscow 119899 RussiaN Larionova - Department of Chemical Enzymology, School of Chemistry Lomonosov Moscow State University Moscow 119899 Russia
- Publication Details
- Biochemistry (Moscow), Vol.66(4), pp.384-389
- Publisher
- Kluwer Academic Publishers-Plenum Publishers; New York
- Identifiers
- 99900546884101842
- Language
- English
- Resource Type
- Journal article