ArticleMethodsX2026
Development of an inexpensive, simple purification method for ω-5 gliadin from wheat flour.
Article in MethodsX, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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3 authors.
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Abstract
ω-5 gliadin is a major causative allergen associated with various types of wheat allergy, including wheat-dependent exercise-induced anaphylaxis. Recently, ω-5 gliadin-deficient wheat has been developed. However, several wheat protein studies do not use standard ω-5 gliadin because its naturally derived form is expensive, and purifying it in-house is time-consuming. Therefore, we sought to develop an inexpensive, simple method for purifying ω-5 gliadin on a small scale.▪We compared ω-5 gliadin-deficient wheat with normal wheat and screened for ω-5 gliadin bands using acid-polyacrylamide gel electrophoresis (A-PAGE) on a mini-slab electrophoresis apparatus.▪The ω-5 gliadin band was excised and sealed in dialysis tubing, and the protein was electroeluted using agarose gel electrophoresis. After electroelution, the eluted solution was filtered, dialyzed, and then freeze-dried.▪The main band of collected proteins migrated at approximately 55 kDa in SDS-PAGE, and the most intense band was identified as ω-5 gliadin using nano-LC-MS/MS.
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