fagopyrum pilus/albumin

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Isolation and identification of antioxidant peptides from tartary buckwheat albumin (Fagopyrum tataricum Gaertn.) and their antioxidant activities.

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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),

2S albumin from buckwheat (Fagopyrum esculentum moench) seeds.

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Sucrose density gradient centrifugation showed that approximately 30% of total buckwheat proteins migrated with a 2S sedimentation coefficient. The main part of that fraction, polypeptides in the range of molecular mass from 8 to 16 kDa, were water soluble and represented albumins. SDS-PAGE analysis

A pitfall in determining the globulin/albumin ratio in amaranth grains.

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In amaranth grains (Amaranthus hypochondriacus L. and Amaranthus cruentus L.), there were two albumin (Alb) fractions, Alb-1 and Alb-2; Alb-1 was extracted with water or 0.5 M NaCl, and Alb-2 was extracted with water after extracting Alb-1 and globulin. The amount of Alb-2 comprised about 30% of the

Application of the 16-kDa buckwheat 2 S storage albumin protein for diagnosis of clinical reactivity.

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BACKGROUND The 16-kDa protein of buckwheat (BW) has been implicated as a major allergen in BW allergy. OBJECTIVE To characterize the 16-kDa allergen and evaluate its clinical significance as an indicator of BW allergy. METHODS Complementary DNA from the 16-kDa allergen was cloned and expressed in

Suppressive Effect of the α-Amylase Inhibitor Albumin from Buckwheat (Fagopyrum esculentum Moench) on Postprandial Hyperglycaemia.

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Inhibiting starch hydrolysis into sugar could reduce postprandial blood glucose elevation and contribute to diabetes prevention. Here, both buckwheat and wheat albumin that inhibited mammalian α-amylase in vitro suppressed blood glucose level elevation after starch loading in vivo, but it had no

Insoluble fraction of buckwheat (Fagopyrum esculentum Moench) protein possessing cholesterol-binding properties that reduce micelle cholesterol solubility and uptake by Caco-2 cells.

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Buckwheat (Fagopyrum esculentum Moench) protein (BWP) exhibits hypocholesterolemic activity in several animal models by increasing fecal excretion of neutral and acidic sterols. In the current study, the ability of BWP to disrupt micelle cholesterol solubility by sequestration of cholesterol was

Surface physicochemical properties of globulin-P amaranth protein.

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Globulin-P, the polymerized 11S amaranth globulin, is composed of 280 kDa unitary molecules (UM, 23%) and aggregates larger than 500 kDa (A, 70%). Antibodies against these proteins were prepared to study their surface characteristics and to assess their homology with other storage proteins. Results

[Buckwheat allergy can cause live-threatening anaphylaxia].

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Alongside with the globalization of the Danish kitchen and the introduction of a larger number of commercial food items containing buckwheat, buckwheat allergy no longer seems to be a rare disease in Denmark. Since buckwheat allergy can cause life-threathening reactions, it is important for medical

Studies on the amino acid and mineral content of buckwheat protein fractions.

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Protein fractions were extracted by successive extraction and analysis method in four buckwheat varieties including Japanese spring buckwheat, Japanese summer buckwheat, Yuqiao No. 1 and Yuqiao 6-21. The amino acid and the mineral content of each protein fraction were also analyzed in this paper.

Immunochemical crossreactivity between globulins from buckwheat and indigo seeds.

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Immunochemical relationships between salt-soluble proteins (albumins plus globulins) from buckwheat and indigo seeds were shown by immunoblot and immunodiffusion analyses using rabbit antisera raised against buckwheat globulins. These antigenic crossreactivities were roughly consistent with their

Molecular cloning of cDNA, recombinant protein expression and characterization of a buckwheat 16-kDa major allergen.

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BACKGROUND Buckwheat is a common food in Japan, Korea and other countries. A candidate major buckwheat allergen, a 16-kDa protein (BWp16), was previously characterized as a pepsin-resistant protein associated with immediate-type allergies to buckwheat. However, whether recombinant BWp16 can react

Characterization of 16-kDa major allergen with α-amylase inhibitor domain in tartary buckwheat seeds.

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Tartary buckwheat (Fagopyrum tataricum, TB) is an important functional food containing proteins with balanced amino acid composition and more flavonoids than common buckwheat (Fagopyrum esculentum, CB). Buckwheat contains highly potent allergens that trigger an allergic reaction via an IgE mediated

[Benzoyl-DL-arginine-p-nitroanilidase from buckwheat seeds. Properties and substrate specificity].

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A proteolytic enzyme, hydrolyzing N-benzoyl-D,L-arginine-p-nitro-anilide (BAPAase), has been isolated from the buckwheat seeds (Fagopyrum esculentum). The enzyme was purified 400-fold and was homogeneous according to isoelectrofocusing and disc electrophoresis in polyacrylamide gel. The molecular

Immunological characterization and mutational analysis of the recombinant protein BWp16, a major allergen in buckwheat.

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Buckwheat allergy is one of the most critical diseases manifested by severe and dangerous symptoms in Japan and other countries. We previously isolated the cDNA encoding protein BWp16, a member of the 2S albumin family with a conserved motif of 8 cysteine (Cys) residues. Comparison of the deduced

Protein-Rich Flours from Quinoa and Buckwheat Favourably Affect the Growth Parameters, Intestinal Microbial Activity and Plasma Lipid Profile of Rats

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In recent years, dietary products with quinoa and buckwheat have attracted attention mostly due to the high nutritive value of their protein fraction. However, their dietary effect on intestinal microbiota activity and related systemic responses are still poorly understood. Therefore, a 2 week study

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