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

33 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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