Results 181 to 190 of about 18,117 (243)

VSL#3 probiotic preparation has the capacity to hydrolyze gliadin polypeptides responsible for Celiac Sprue probiotics and gluten intolerance

open access: bronze, 2005
Maria De Angelis   +8 more
openalex   +1 more source

Celiac disease: antibody recognition against native and selectively deamidated gliadin peptides.

open access: bronze, 2001
Mabel Aleanzi   +4 more
openalex  

Processing of mitochondrial precursor proteins [PDF]

open access: yes, 1984
Neupert, Walter, Schmidt, Bernd
core  
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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   +3 more
openaire   +5 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.
John F. Woodley, Gordon Bruce
openaire   +3 more sources

Quantification of Gliadin by Flow Cytometry

Cereal Chemistry, 2004
Gliadin 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
openaire   +4 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.
W. T. J. M. Hekkens   +2 more
openaire   +3 more sources

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