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- Title
The anionic protease inhibitor BWI-1 from buckwheat seeds. Kinetic properties and possible biological role.
- Authors
Dunaevsky, Yakov E.; Gladysheva, Inna P.; Pavlukova, Ekaterina B.; Beliakova, Galina A.; Gladyshev, Dmitry P.; Papisova, Alla I.; Larionova, Natalja I.; Belozersky, Mikhail A.
- 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.
- Subjects
FILAMENTOUS fungi; PROTEASE inhibitors; TRYPSIN; CHYMOTRYPSIN; AMINO acid sequence; GERMINATION
- Publication
Physiologia Plantarum, 1997, Vol 101, Issue 3, p483
- ISSN
0031-9317
- Publication type
Article
- DOI
10.1111/j.1399-3054.1997.tb01027.x