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Sivu 1 alkaen 30 tuloksia
Analysis of avenin proteins and the expression of their mRNAs in developing oat seeds.
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We have isolated and characterized cDNA clones encoding avenins, the prolamine storage proteins of oat seeds. Sequence analysis shows that avenins are a related group of polypeptides and that their mRNAs differ from each other by point mutations and small insertions and deletions. Avenin proteins
Immunocrossreactivity of antisera against grain prolamines of wheat, rye, barley and oats.
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Prolamines extracted from wheat (gliadin), rye (secalin), barley (hordein) and oats (avenin) were used to raise antibodies in rabbits. The four prolamines were separated by SDS-PAGE and blotted onto nitrocellulose. The immunocrossreactivity of the separated prolamines with the four antisera was
Mapping Coeliac Toxic Motifs in the Prolamin Seed Storage Proteins of Barley, Rye, and Oats Using a Curated Sequence Database
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Wheat gluten, and related prolamin proteins in rye, barley and oats cause the immune-mediated gluten intolerance syndrome, coeliac disease. Foods labelled as gluten-free which can be safely consumed by coeliac patients, must not contain gluten above a level of 20 mg/Kg. Current immunoassay methods
Screening of gluten avenins in foods by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
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The first procedure capable of analysing gluten avenins in gluten-free food samples aimed at the diet control of coeliac patients is described. The method is based on the direct observation of the characteristic avenin mass pattern, around 20-30 kDa, as revealed by matrix-assisted laser
Placement of loci for avenins and resistance to Puccinia coronata to a common linkage group in Avena strigosa.
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Alcohol-soluble seed storage proteins of oat (avenins) were extracted from two diploid accessions representing the A genome and separated by high-resolution acid polyacrylamide gel electrophoresis. Polymorphisms were detected for three clearly resolved protein bands. Linkage analysis of 88 F2:3
Preparation and Characterization of Avenin-Enriched Oat Protein by Chill Precipitation for Feeding Trials in Celiac Disease.
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The safety of oats for people with celiac disease remains unresolved. While oats have attractive nutritional properties that can improve the quality and palatability of the restrictive, low fiber gluten-free diet, rigorous feeding studies to address their safety in celiac disease are needed.
Ingestion of oats and barley in patients with celiac disease mobilizes cross-reactive T cells activated by avenin peptides and immuno-dominant hordein peptides.
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Celiac disease (CD) is a common CD4(+) T cell mediated enteropathy driven by gluten in wheat, rye, and barley. Whilst clinical feeding studies generally support the safety of oats ingestion in CD, the avenin protein from oats can stimulate intestinal gluten-reactive T cells isolated from some CD
No induction of anti-avenin IgA by oats in adult, diet-treated coeliac disease.
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OBJECTIVE
Coeliac disease is effectively treated with a gluten-free diet devoid of wheat, rye, barley and related cereals. Oats has until recently also been considered harmful but is now allowed in several countries. We have, however, identified three adult coeliac disease patients who developed a
Isolation and characterization of gluten protein types from wheat, rye, barley and oats for use as reference materials.
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Gluten proteins from wheat, rye, barley and, in rare cases, oats, are responsible for triggering hypersensitivity reactions such as celiac disease, non-celiac gluten sensitivity and wheat allergy. Well-defined reference materials (RM) are essential for clinical studies, diagnostics, elucidation of
Selective identification by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry of different types of gluten in foods made with cereal mixtures.
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The gluten toxic fractions responsible for the mucosal damage in coeliac disease (CD), so-called gliadins, hordeins, secalins and avenins from a large number (30-40) of wheat, barley, rye and oats cultivars respectively, have been mass analyzed by matrix-assisted laser desorption/ionization
Relation of antigenic structure of cereal proteins to their toxicity in coeliac patients.
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Unfractionated gliadin and its alpha-, beta-, gamma- and omega-gliadin subfractions were used as rabbit immunogens. The antisera were characterized by (1) Ouchterlony double diffusion, (2) binding of 125I-labelled gliadin subfractions, (3) inhibition by several gliadin subfractions of binding
An innovative sandwich ELISA system based on an antibody cocktail for gluten analysis.
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A cocktail sandwich ELISA based on the employ of two monoclonal antibodies (MAbs) as coating antibodies and a third MAb conjugated to horseradish peroxidase has been developed for the analysis of gluten in foods. Given that each MAb displays a wide specificity spectrum for wheat, barley, rye and
Measurement of wheat gluten and barley hordeins in contaminated oats from Europe, the United States and Canada by Sandwich R5 ELISA.
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OBJECTIVE
We have investigated the extent of contamination with wheat, barley, rye or a mixture of these cereals in a large number of grains and commercial oats. We have also attempted to identify the type of cereal contaminant.
METHODS
Sandwich R5 ELISA (using either gliadins or hordeins as
X6: A Novel Antibody for Potential Use in Gluten Quantification
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Gliadin is a fraction of gluten, known to trigger celiac disease in susceptible people. To date, the life-long gluten-free diet is used for the prevention of this disease. Hence, methods for gluten control in foods are of significant importance. Being one of the most-used methods used for this
Gluten sensitivities and the allergist: Threshing the grain from the husks.
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"Gluten sensitivity" has become commonplace among the public. Wheat allergy (WA) and celiac disease (CD) are well-defined entities, but are becoming a fraction of individuals following a gluten-free diet (GFD). Wheat allergy has a prevalence of <0.5%. Wheat, specifically its omega-5 gliadin
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