fagopyrum urophyllum/protease

The complete amino acid sequence of protease inhibitor BWI-1 from buckwheat (Fagopyrum esculentum Moench) seeds has been established by automatic Edman degradation and mass spectrometry. The molecule of the inhibitor consists of 69 amino acid residues, with a molecular mass calculated as 7743.8 Da.

Buckwheat is a popular food material in many Asian countries and it contains major allergenic proteins. This study was performed to analyze the effects of hydrolysis with alkaline protease following high hydrostatic pressure (HHP) treatment on the IgE binding of buckwheat protein. Extracted

The complete amino acid sequence of protease inhibitor BWI-4a from buckwheat (Fagopyrum esculentum Moench) seeds, consisting of 67 amino acid residues with a single disulfide bond, has been established by Edman degradation in combination with matrix-assisted laser desorption ionization

The complete amino acid sequence of the protease inhibitor BWI-4a from buckwheat (Fagopyrum esculentum Moench) seeds has been established by automated Edman degradation in combination with MALDI-TOF mass spectrometry. The inhibitor molecule consists of 67 amino acid residues with a single disulfide

Complete amino acid sequence of IT1 protease inhibitor and partial amino acid sequences of IT2 and IT4 protease inhibitors from buckwheat Fagopyrum esculentum Moench seeds were determined by automatic Edman degradation and mass spectrometry. IT1 inhibitor comprises 69 amino acid residues and its

The buckwheat protease inhibitor designated BWI-1, a member of the potato inhibitor I family, inhibits trypsin, chymotrypsin, and subtilisin, whereas the buckwheat protease inhibitor designated BWI-2a, a novel protease inhibitor homologous to the vicilin family, inhibits only trypsin. We examined

Three protease inhibitors (BWI-1, BWI-2 and BWI-4) from buckwheat seeds were purified to homogeneity and characterized. Their molecular masses were 7.7-9.2 kDa according to gel-filtration and mass spectrometry. Amino acid analysis revealed a high content of glutamic acid and valine and a low content

Plants are known to have many secondary metabolites and phytochemical compounds which are highly explored at biochemical and molecular genetics level and exploited enormously in the human health care sector. However, there are other less explored small molecular weight proteins, which inhibit

Preparations of new low molecular weight protein inhibitors of serine proteinases have been obtained from buckwheat Fagopyrum esculentum seeds by chromatography of seed extracts on trypsin-Sepharose 4B, Mono-Q and Mono-S ion-exchangers. Their molecular masses, determined by mass spectrometry, were

The possibility to use agrobacterial transformation of leaf discs to produce resistance to bacterial infections in tobacco and potato plants by introduction of a single gene encoding the serine proteinase inhibitor BWI-1a (ISP) from buckwheat seeds is shown. All studied PCR-positive transgenic

The stability of marker nptII and target gene of serine proteinase inhibitor BWI-1a (ISP) from buckwheat seeds after agrobacterial transformation in the new foreign genome environment has been investigated. Different vegetative and seed progeny of self-pollinated transgenic tobacco was studied after

Common buckwheat (Fagopyrum esculentum Moench) was foliarly sprayed with a water solution containing 10 mg Se(VI) L(-1) at the beginning of flowering. The total Se content in plant parts in the untreated group was low, whereas in the Se-sprayed group it was approximately 50- to 500-fold higher,

Tartary buckwheat (Fagopyrum tataricum Gaertn.) albumin was hydrolyzed by alkaline protease, and three new antioxidant peptides (P1, P2, and P3) were successfully separated from the hydrolysate (TBAH). The sequences of the three antioxidant peptides were Gly-Glu-Val-Pro-Trp (GEVPW),

OBJECTIVE Due to its beneficial health effects, use of buckwheat has shown a continuous increase, and concerns regarding the allergic property of buckwheat have also increased. This study was conducted for evaluation of the hydrolytic effects of seven commercial proteases on buckwheat allergens and

It has been demonstrated that buckwheat seeds contain a proteinaceous inhibitor of trypsin and chymotrypsin. The isolation technique consisted in extraction of the seed flour with water, ammonium sulfate fractionation, isoelectric precipitation, gel filtration on Sephadex G-75 and ion-exchange