Gliadin Deamidated gliadin is produced by acid or enzymatic treatment of gluten. The enzyme tissue transglutaminase converts some of the abundant glutamines to glutamic acid. This is done because gliadins are soluble in alcohol and cannot be mixed with other foods (like milk) without changing the foods' qualities. Deamidated gliadin is soluble in water. The cellular immunity to deamidated α-/β-gliadin is much greater than α/β-gliadin and can result in symptomatic gluten-sensitive enteropathy. Celiac disease is a chronic, immune-mediated intestinal disorder, in which the body becomes intolerant to gliadin, which is a component of gluten. Individuals with celiac disease exhibit a lifelong
Gluten immunochemistry include: LTP (albumin/globulin), thioredoxin-hB, and wheat flour peroxidase. A particular 5 residue peptide, Gln-Gln-Gln-Pro-Pro motif, has been found to be a major wheat allergen. New immunogenic motifs appear in the literature almost monthly and new gliadin and "Triticeae" protein sequences appear that contain these motifs. The HLA DQ2.5 restricted peptide "I I Q P Q Q P A Q" produced approximately 50 hits of identical sequences in NCBI-Blast search is one of a several dozen known motifs whereas only a small fraction of Triticeae gluten variants have been examined. For this reason the immunochemistry is best discussed at the level