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The anionic protease inhibitor BWI‐1 from buckwheat seeds. Kinetic properties and possible biological role
Author(s) -
Dunaevsky Yakov E.,
Gladysheva Inna P.,
Pavlukova Ekaterina B.,
Beliakova Galina A.,
Gladyshev Dmitry P.,
Papisova Alla I.,
Larionova Natalja I.,
Belozersky Mikhail A.
Publication year - 1997
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1997.tb01027.x
Subject(s) - chymotrypsin , protease , biochemistry , mycelium , amino acid , chemistry , trypsin , cathepsin g , enzyme , hydrolysis , germination , biology , elastase , botany
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 n M , 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 P j 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.