Results 131 to 140 of about 10,068 (188)

IgA Subclasses and Free Light Chains in Celiac Disease: A Pilot Study. [PDF]

Int J Mol Sci
Carnazzo V, Grieco V, Basile V, Redi S, Marino M, Ciasca G, Bondanini F, Basile U.   +7 more
europepmc   +1 more source

Mitigative effects of carboxymethyl chitosan on the deterioration of gliadin tractility in frozen rice dough during frozen storage. [PDF]

Food Chem X
Dong W, Wu Y, Zhang G, Wei Q.
europepmc   +1 more source

Is There a Future Without Gluten Restrictions for Celiac Patients? Update on Current Treatments. [PDF]

Nutrients
Girbal-González M, Pérez-Cano FJ.
europepmc   +1 more source

IFN-γ signaling stimulates intestinal crypt hyperplasia in celiac disease. [PDF]

J Clin Invest
Weingarden AR.
europepmc   +1 more source

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Foaming Properties of Wheat Gliadin

Journal of Agricultural and Food Chemistry, 2011
We 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.
Kristof Brijs, Jan Delcour
exaly   +3 more sources

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;
Charles Hedgcoth
exaly   +2 more sources

Gliadin Characterization by Sans and Gliadin Nanoparticle Growth Modelization

Journal of Nanoscience and Nanotechnology, 2006
Nanosized colloidal carriers can ensure a controlled and targeted therapeutic substances delivery. The original contribution of this work was to use biopolymers of vegetable source, which are an interesting alternative to synthetic polymers. The aim of this study was to prepare submicronic particles from wheat proteins: Gliadins extracted from gluten.
Orecchioni, Anne-Marie, Duclairoir, Cécile, Renard, Denis, Nakache, Evelyne   +3 more
openaire   +4 more sources

An accurate fluorometric method to measure the breakdown of gliadin and gliadin peptides

Clinica Chimica Acta, 1981
A 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.
G, Bruce, J F, Woodley
openaire   +2 more sources

Lysosomal damage by gliadin and gliadin peptides; An activity not related to coeliac disease

Clinica Chimica Acta, 1979
Rat-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.
F W, de Rooij, C P, van den Aarsen, W T, Hekkens   +2 more
openaire   +2 more sources

Biochemical and molecular characterization of gliadins

Molecular Biology, 2006
Gliadins 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.
P F, Qi, Y M, Wei, Y W, Yue, Z H, Yan, Y L, Zheng   +4 more
openaire   +2 more sources