The anionic protease inhibitor BWI-1 from buckwheat seeds. Kinetic properties and possible biological role

  • Yakov E. Dunaevsky
  • , Inna P. Gladysheva
  • , Ekaterina B. Pavlukova
  • , Galina A. Beliakova
  • , Dmitry P. Gladyshev
  • , Alla I. Papisova
  • , Natalja I. Larionova
  • , Mikhail A. Belozersky

Research output: Contribution to journalArticlepeer-review

40 Scopus citations

Abstract

Kinetic characteristics and effects on the growth of filamentous fungi of one of the main anionic protease inhibitors, BWI-1, isolated from buckwheat seeds, have been studied. The inhibition constants of bovine trypsin, chymotrypsin and cathepsin G from human granulocytes with BWI-1 were found to be 1.1, 67 and 200 nM, respectively. Analysis of the amino acid sequence of BWI-1 in the vicinity of the reactive site revealed its homology to the potato proteinase inhibitor I family. It is suggested that the inability of BWI-1 to bind elastase of human granulocytes is due to the basic nature of the amino acid residue (Arg) at the P1 position in its reactive site. It was demonstrated that BWI-1 was able to suppress the germination of the spores and the growth of the mycelium of two filamentous fungi.

Original languageEnglish (US)
Pages (from-to)483-488
Number of pages6
JournalPhysiologia Plantarum
Volume101
Issue number3
DOIs
StatePublished - 1997
Externally publishedYes

Keywords

  • Buckwheat
  • Fagopyrum esculentum
  • Filamentous fungi
  • Proteinase
  • Reactive site
  • Seeds
  • Trypsin inhibitor

ASJC Scopus subject areas

  • Physiology
  • Genetics
  • Plant Science
  • Cell Biology

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