Conjugation of the bowman-birk soybean proteinase inhibitor with hydroxyethylstarch

Nathalia I. Larionova, Stepan S. Vartanov, Nadezhda V. Sorokina, Inna P. Gladysheva, Sergey D. Varfolomeyev

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


The classical Bowman-Birk soybean proteinase inhibitor was modified by hydroxyethylstarch. The modified inhibitor retained the capacity for simultaneous binding of trypsin and human leukocyte elastase. The inhibition constants, Ki, of bovine trypsin, α-chymotrypsin and human leukocyte elastase (HLE) increased not more than 10-, 1.5-, and 20-fold, respectively, on modification of the inhibitor. The less effective inhibition is presumably due to the steric hindrance brought about by the conjugation with polysaccharide molecules. The results obtained indicate the pronounced structure differences of the binding regions for trypsin and chymotrypsin/leukocyte elastase in the modified preparation.

Original languageEnglish (US)
Pages (from-to)175-182
Number of pages8
JournalApplied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology
Issue number2-3
StatePublished - 1997
Externally publishedYes


  • Bowman-Birk soybean inhibitor
  • Conjugate
  • Hydroxyethylstarch
  • Leukocyte elastase
  • Modification

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology


Dive into the research topics of 'Conjugation of the bowman-birk soybean proteinase inhibitor with hydroxyethylstarch'. Together they form a unique fingerprint.

Cite this