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Enzyme-linked immunosorbent assays (ELISAs) are widely used to determine gluten contamination in gluten-free and low gluten food samples. ELISA assays developed using monoclonal antibodies against known toxic peptides have an advantage in the identification of toxic prolamin content in protein extracts of different food samples, as well as raw materials. R5 and G12 monoclonal antibodies specific for two known toxic peptides used in commercially available gluten ELISA assays were applied to test toxic peptide contents in wheat relatives and wild wheat species with different genome composition and complexity. Although the R5 peptide content showed some correlation with ploidy levels in Triticum species, there was a high variance among Aegilops species. Some of the analysed diploid Aegilops species showed extremely high R5 peptide contents. Based on the bioinformatics analyses, the R5 peptide was present in most of the sulphur rich prolamins in all the analysed species, whereas the G12 epitope was exclusively present in alpha gliadins. High variation was detected in the position and frequency of epitopes in sequences originating from the same species, thus highlighting the importance of genotypic variation within species. Identification of new prolamin alleles of wheat relatives and wild wheat species is of great importance in order to find germplasm for special end-use quality purposes as well as development of food with reduced toxicity.

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sensitive detection of coeliac disease toxic prolamins. Analytica Chimica Acta 551 :105–114. O’sullivan C.K. Monoclonal antibody-based competitive assay for the sensitive detection of

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1229 1234 Anderson, R.P., Degano, P., Godkin, A.J., Jewell, D.P., Hill, A.V.S. 2000. In vivo antigen challenge in celiac disease identifies a single transglutaminase

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784 Endres, W., Wuttge, B. (1978) Occurrence of secondary cystathioninuria in children with inherited metabolic disorders, liver diseases, neoplasms, cystic fibrosis and celiac disease. Eur

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.P., Hill, A.V.S. 2000. In vivo antigen challenge in celiac disease identifies a single transglutaminase-modified peptid as the dominant A gliadin T-cell epitope. Nature (Med). 6 :337–342. Hill A

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Cereal Research Communications
Authors: R. Redaelli, G. Scalfati, R. Ciccoritti, P. Cacciatori, E. De Stefanis, and D. Sgrulletta

Arentz-Hansen, H., Fleckenstein, B., Molberg, O., Scott, H., Koning, F. et al. 2004. The molecular basis for oat intolerance in celiac disease patients. PloS Med. 1 :e1. Koning F. The

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., Maialetti, F., Gazza, L., Silano, M., Dessi, M., De Vincenzi, M., Pogna, N.E. 2007. Environmental factors of celiac disease: Cytotoxicity of hulled wheat species Triticum monococcum, T. turgidum ssp. dicoccum and T. aestivum ssp. spelta . J. Gastroen

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Cereal Research Communications
Authors: J. Bystrická, A. Vollmannová, A. Kupecsek, J. Musilová, Z. Poláková, I. Čičová, and T. Bojňanská

1801 1804 Kupper, C. 2005. Dietary guidelines and implementation for celiac disease. Gastroenterology 128 :121–127. Kupper C

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mucosal vitamin C concentrations are highly reduced [ 56 ]. Furthermore, when applying vitamin C to duodenal explants derived from patients suffering from coeliac disease due to a hypersensitivity reaction to wheat gliadin and similar proteins from rye and

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Arentz-Hansen, E.H., McAdam, S.N., Molberg, O., Kristiansen, C., Sollid, L.M. 2000. Production of a panel of recombinant gliadins for the characterisation of T cell reactivity in coeliac disease. Gut 46 :46

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