The anionic protease inhibitor BWI-1 from buckwheat seeds. Kinetic properties and possible biological role
| Autor: | Inna P. Gladysheva, Dmitry P. Gladyshev, Yakov E. Dunaevsky, G. A. Beliakova, Natalja I. Larionova, Alla I. Papisova, Ekaterina B. Pavlukova, Mikhail A. Belozersky |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
chemistry.chemical_classification
Protease Chymotrypsin biology Physiology Trypsin inhibitor medicine.medical_treatment fungi Cell Biology Plant Science General Medicine Cathepsin G Protease inhibitor (biology) chemistry.chemical_compound Enzyme Biochemistry chemistry Enzyme inhibitor medicine biology.protein Genetics Peptide sequence medicine.drug |
| Zdroj: | Physiologia Plantarum. 101:483-488 |
| ISSN: | 1399-3054 0031-9317 |
| DOI: | 10.1034/j.1399-3054.1997.1010305.x |
| Popis: | Kinetic characteristics and effects on the growth of filamentous fungi of one of the main anionic protease inhibitors, BWI-I, 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-I to bind elastase of human granulocytes is due to the basic nature of the amino acid residue (Arg) at the P 1 position in its reactive site. It was demonstrated that BWI-I was able to suppress the germination of the spores and the growth of the mycelium of two filamentous fungi. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text