Efficiency and Limitations of Immunochemical Assays for the Testing of Gluten-free Foods

Efficiency and Limitations of Immunochemical Assays for the Testing of Gluten-free Foods This review considers the various immunochemical assays developed for gluten quantification and their feasibility for testing gluten-free food consumed by patients with coeliac disease. The first part concerns the major requirements of these assays: (a) detection of prolamins from the different cereals involved in gluten intolerance (wheat, rye, barley and oats) and avoidance of cross-reactions with prolamins from maize, rice, etc.; and (b) sensitive detection of native proteins as well as those denatured by cooking or other treatments. The second part evaluates several immunochemical assays in terms of their specificity, sensitivity and dependence on heat treatments. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Cereal Science Elsevier

Efficiency and Limitations of Immunochemical Assays for the Testing of Gluten-free Foods

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Publisher
Elsevier
Copyright
Copyright © 1999 Academic Press
ISSN
0733-5210
eISSN
1095-9963
D.O.I.
10.1006/jcrs.1999.0268
Publisher site
See Article on Publisher Site

Abstract

This review considers the various immunochemical assays developed for gluten quantification and their feasibility for testing gluten-free food consumed by patients with coeliac disease. The first part concerns the major requirements of these assays: (a) detection of prolamins from the different cereals involved in gluten intolerance (wheat, rye, barley and oats) and avoidance of cross-reactions with prolamins from maize, rice, etc.; and (b) sensitive detection of native proteins as well as those denatured by cooking or other treatments. The second part evaluates several immunochemical assays in terms of their specificity, sensitivity and dependence on heat treatments.

Journal

Journal of Cereal ScienceElsevier

Published: Sep 1, 1999

References

  • Considering wheat, rye and barley proteins as aids to carcinogens
    Hoggan, R.
  • Matrix-assisted laser desorption/ionization time-of-flight mass spectrometric micro-analysis: the first non-immunological alternative attempt to quantify gluten gliadins in food samples
    Camafeita, E.; Alfonso, P.; Mothes, T.; Méndez, E.
  • Analysis of wheat storage proteins by exhaustive sequential extraction followed by RP-HPLC and nitrogen determinations
    Nicolas, Y.; Martinant, J.P.; Denery-Papini, S.; Popineau, Y.
  • Heterogeneous reactivity patterns of HLA-DQ-restricted, small intestinal T-cell clones from patients with celiac disease
    Lundin, K.E.A; Sollid, L.M.; Anthonsen, D.; Noren, O.; Molberg, O.; Thorsby, E.; Sjöström, H.
  • Coeliac activity of the gliadin peptides CT-1 and CT-2
    Wieser, H.; Belitz, H.D.; Idar, D.; Ashkenazi, A.
  • A major wheat allergen has a Gln-Gln-Gln-Pro-Pro motif identified as an IgE-binding epitope
    Tanabe, S.; Arai, S.; Yanagihara, Y.; Mita, H.; TakaÍhashi, K.; Watanabe, M.
  • A sensitive monoclonal-antibody-based test for gluten detection: quantitative immunoassay
    Skerritt, J.H.

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