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
Wheat allergy high molecular weight glutenin subunit, and similar proteins in other "Triticeae" genera, enter the blood stream during exercise where they cause acute asthmatic or allergic reaction. One recent study of ω-gliadins demonstrated these gliadins are more similar to the bulk of oat avenins than α/β or γ gliadins but, so far, oat avenins have not been linked to WDEIA. Wheat may specifically induce WDEIA and certain chronic urticaria because the anti-gliadin IgE detects ω-gliadins expressed by most of the Gli-B1 alleles, but prolamins extracted from rye or wheat/rye translocates invoke almost no responses. The Gli-B1 gene in wheat, "Triticum aestivum",