Results 191 to 200 of about 12,298 (216)

A cappelle‐desprez β‐gliadin

Journal of the Science of Food and Agriculture, 1977
AbstractA β‐gliadin from Cappelle‐Desprez wheat has been purified sufficiently to be analysed. Its amino acid composition is typical of the gliadin class. The molecule appears to be a single polypeptide chain with no carbohydrate or SH groups and a molecular weight of 38 000.
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The chemistry of gliadin

1978
Becarri, in 1745, and Einhof, in 1805, were the first to study the proteins present in wheat flour, but the name ‘gliadin’ was not known until 1820 when Taddei used this name to describe the alcohol-soluble protein components of flour. Since then, an ever-increasing amount of literature has appeared on gliadin. Up to 1970, Chemical Abstracts quotes 536
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Nucleotide sequence of a γ gliadin gene: Comparisons with other γ gliadin sequences show the structure of γ gliadin genes and the general primary structure of γ gliadins

Plant Science, 1988
Abstract A low stringency screening of a wheat ( Triticum aestivum L.) genomic library produced three types of γ gliadin clones. The sequence of one clone, λ10–20, encoded a γ gliadin of 34.3 kDa. Comparisons of this protein with the proteins encoded by other γ gliadin DNA sequences revealed a general γ gliadin structure: a 19-residue signal peptide;
Kay Scheets, Charles Hedgcoth
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Isolation of a cappelle‐desprez gliadin

Journal of the Science of Food and Agriculture, 1975
AbstractA Cappelle‐Desprez gliadin, previously unreported, has been isolated. It appears to be a single‐chain protein with a molecular weight of only 18 000, considerably lower than that of any other gliadin so far isolated. Its amino acid composition, though broadly typical of the class, has surprising characteristics, such as 7 Met, 7 CySSCy, but ...
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Some observations on the electrophoresis of gliadin

Biochimica et Biophysica Acta, 1954
Abstract Gliadin has been separated into two fractions by a new method and both fractions have been subjected to electrophoretic analysis in different buffers. It has been concluded that gliadin is a mixture of at least four electrophoretically distinct proteins.
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Enzyme-linked immunosorbent assay for wheat α-gliadin and whole gliadin

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
Abstract Competitive and noncompetitive heterogeneous enzyme immunoassays for quantitation of A-gliadin and whole gliadin have been developed using antigen-, antibody- or Protein A-horseradish peroxidase conjugates. The efficiencies of three different coupling procedures were compared.
Erich Baumgartner, Franziska Fritschy, Helena Windemann   +2 more
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Study on the interaction between gliadins and a coumarin as molecular model system of the gliadins–anthocyanidins complexes

Food Chemistry, 2013
To clarify the conformational changes of gliadins (Glia) upon complexation with anthocyanidins (in particular cyanidin, Cya), the interaction of Glia with a coumarin derivative (3-ethoxycarbonylcoumarin, 3-EcC), having a benzocondensed structure similar to that of Cya, has been investigated by NMR, IR, and Raman spectroscopy under acidic and neutral ...
TOZZI, SILVIA, ZANNA, NICOLA, TADDEI, PAOLA   +2 more
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A sandwich enzyme immunoassay for wheat gliadin

Journal of Immunological Methods, 1986
A sandwich double antibody solid-phase enzyme immunoassay (EIA) that can detect and quantitate gliadin is described. Quantitative analysis could be carried out in the range of 5-400 ng/ml and the assay was more sensitive than inhibition EIA. Gliadin possessed weak cross-reactivity with oats, maize and rice prolamines.
TRONCONE, RICCARDO, VITALE M, DONATIELLO A, FARRIS E, ROSSI G, AURICCHIO S.   +5 more
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Anti-gliadin Antibodies

Journal of Pediatric Gastroenterology and Nutrition, 1991
TRONCONE, RICCARDO, FERGUSON A.
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Gliadin Detection by Immunoassay

2017
Immunoassays are very sensitive and efficient tests commonly used to identify a specific protein. Examples of applications in the food industry include identification of proteins expressed in genetically modified foods, allergens, or proteins associated with a disease, including celiac disease. Celiac disease can be managed if the consumer avoids foods
Qinchun Rao, Y. H. Peggy Hsieh
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