Human leukocyte elastase inhibition by Bowman-Birk soybean inhibitor. Discrimination of the inhibition mechanisms

Natalia I. Larionova, Inna P. Gladysheva, Dimitri P. Gladyshev

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

The reaction between human leukocyte elastase and soybean Bowman-Birk inhibitor has been studied. The inhibition was found to be due to slow tight binding of the inhibitor. The interaction of BBI with HLE was shown to involve two steps: the rapid formation of an initial EI complex, with a K(i) of 28 nM, followed by a slow equilibrium conversion to a tighter-binding EI* complex with a final K(i)* of 2.3 nM. At pH 7.5 and 25°C, k(on) was 3.5 x 104 M-1 s-1 and k(off) was 1.0 x 10-4 s-1.

Original languageEnglish (US)
Pages (from-to)245-248
Number of pages4
JournalFEBS Letters
Volume404
Issue number2-3
DOIs
StatePublished - Mar 10 1997
Externally publishedYes

Keywords

  • Bowman-Birk soybean inhibitor
  • Human leukocyte elastase
  • Inhibition constant
  • Kinetic constant

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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