Results 141 to 150 of about 10,068 (188)
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Quantification of Gliadin by Flow Cytometry
Cereal Chemistry, 2004Gliadin is a heterogeneous group of alcohol-soluble wheat storage proteins, comprising ≈50% of the gluten proteins (Campbell et al 1987; Fido et al 1997). Gliadin influences important baking properties of wheat, in particular loaf volume (Weegels et al 1994; Khatkar et al 2002) and water absorption (Dong et al 1992).
CAPPARELLI, ROSANNA +6 more
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Correlation between gliadin bands
Theoretical and Applied Genetics, 1983Starch gel electrophoresis of gliadins was carried out for 37 bread wheat cultivars chosen for their distant relationships. Simple correlations were calculated between each of the 41 bands (variates) observed with these wheats. It was found that a band is usually negatively correlated with the two neighbouring mobility bands.
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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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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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Some observations on the electrophoresis of gliadin
Biochimica et Biophysica Acta, 1954Abstract 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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Separation and characterization of α-gliadin fractions
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971Abstract The α-gliadin protein fraction (from hard red winter wheat) obtained by an ultracentrifugation technique has been further fractionated into four subfractions by ion exchange on sulfoethyl cellulose in a solvent that contained 8 M urea. The subfractions differ in electrophoretic mobility upon gel electrophoresis at pH 3.3.
S G, Platt, D D, Kasarda
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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 +2 more
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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 +2 more
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Isolation of a cappelle‐desprez gliadin
Journal of the Science of Food and Agriculture, 1975AbstractA 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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Journal of Pediatric Gastroenterology and Nutrition, 1991
TRONCONE, RICCARDO, FERGUSON A.
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TRONCONE, RICCARDO, FERGUSON A.
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