Results 181 to 190 of about 12,298 (216)
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An accurate fluorometric method to measure the breakdown of gliadin and gliadin peptides
Clinica Chimica Acta, 1981A simple and accurate method is described to measure the breakdown of gliadin and gliadin peptides. It involves measuring the release of the predominant amino acids glutamine and glutamic acid using a fluorometric double enzyme assay and contains none of the problems normally associated with previously used techniques.
John F. Woodley, Gordon Bruce
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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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Lysosomal damage by gliadin and gliadin peptides; An activity not related to coeliac disease
Clinica Chimica Acta, 1979Rat-liver lysosomes have been used to determine the toxicity of gliadin fractions in relation to coeliac disease. In this study we compared the activity in acid phosphatase release from rat-liver lysosomes by casein, gliadin and by their peptic-tryptic digests. The release of acid phosphatase is not specific for gliadin.
W. T. J. M. Hekkens+2 more
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Colloid and Polymer Science, 2016
Bio-derived, fully biodegradable closed-cell micro- and nanocellular foams were generated from gliadin. Gliadin, an abundantly available wheat storage protein, was extracted with aqueous ethanol from wheat gluten. For the newly developed foaming process, dry gliadin powder was plasticized by equal volumes of water and ethanol resulting in a ...
Silke Quester+2 more
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Bio-derived, fully biodegradable closed-cell micro- and nanocellular foams were generated from gliadin. Gliadin, an abundantly available wheat storage protein, was extracted with aqueous ethanol from wheat gluten. For the newly developed foaming process, dry gliadin powder was plasticized by equal volumes of water and ethanol resulting in a ...
Silke Quester+2 more
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Surface Films of Gliadin [PDF]
MITCHELL1 has reported that under suitable conditions proteins can be spread from a solution to give films the force-area curves of which show a sharp transition point in the region of 1–2 dynes/cm., the extrapolated areas of the two distinct portions of the curve being approximately 0.3 and 0.7 × 10−7gm. /sq. cm. respectively.
T. W. J. Taylor, G. I. Jenkins
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Journal of Food Science, 1991
ABSTRACTCrude wheat gliadin from acetic acid solution showed lower water sorption by pulse and frontal Inverse Gas Chromatography methods as compared to a static method but the pulse data for a highly purified Ponca wheat gliadin from ethanol agreed with static data for crude gliadin.
Henryk Daun+2 more
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ABSTRACTCrude wheat gliadin from acetic acid solution showed lower water sorption by pulse and frontal Inverse Gas Chromatography methods as compared to a static method but the pulse data for a highly purified Ponca wheat gliadin from ethanol agreed with static data for crude gliadin.
Henryk Daun+2 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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Biochemical and molecular characterization of gliadins
Molecular Biology, 2006Gliadins account for about 40-50% of the total proteins in wheat seeds and play an important role on the nutritional and processing quality of flour. Usually, gliadins could be divided into alpha- (alpha/beta-), gamma- and omega-groups, whereas the low-molecular-weigh (LMW) gliadins were novel seed storage proteins.
Yuan-Wen Yue+4 more
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Polymorphism of gliadin and unusual gliadin alleles in Triticum boeoticum
Genome, 1992More than 50 gliadin electrophoretic patterns (Al-lactate, pH 3.1) have been found in a collection of 60 T. monococcum L. ssp. boeoticum accessions. Analyses of F2 seeds of the two intraspecies crosses revealed two unlinked gliadin-coding loci (Gli-A1bt and Gli-A2bt) in each genotype studied.
E. V. Metakovsky, S. K. Baboev
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Foaming Properties of Wheat Gliadin
Journal of Agricultural and Food Chemistry, 2011We studied gliadin solubility, surface tension and foam behavior, and the presence of different gliadin types in gliadin aqueous solutions and foams as a function of pH. Gliadin has excellent foaming properties only at neutral and alkaline pH. Its solubility is minimal near neutral pH, while almost complete at acidic and alkaline pH.
Bert G. Thewissen+3 more
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