Results 181 to 190 of about 14,422 (235)

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

J Clin Invest
Weingarden AR.
europepmc   +1 more source

Bifidobacteria and Celiac Disease: Mechanisms of Probiotic Action in Reducing Gluten-Induced Cytotoxicity and Inflammation. [PDF]

Mol Nutr Food Res
Scherer TC, De Marco I, Ferreira NRC, Pimentel TC, Magnani M, Hassemer GS, Nascimento ABD, Verruck S.   +7 more
europepmc   +1 more source

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 A Delcour
exaly   +4 more sources

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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

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.
openaire   +2 more sources