Gliadin the formation of gluten. They are slightly soluble in ethanol and contain only intramolecular disulfide links. They also cause some of the best examples of food-derived pathogenesis. People with gluten-sensitive enteropathy (the severe form of which is celiac disease) are sensitive to α, β, and γ gliadins. Those with WD urticaria and Baker's asthma are sensitive to ω-gliadins. Gliadin can also serve as a useful delivery method for sensitive enzymes (such as superoxide dismutase, which is fused with gliadin to form glisodin) – this helps protect them from stomach acids that cause breakdown. For useful description of the gliadins see:
Prolamin disease in genetically predisposed individuals. Prolamin Prolamins are a group of plant storage proteins having a high proline content and found on plant materials mainly like in the seeds of cereal grains: wheat (gliadin), barley (hordein), rye (secalin), corn (zein), sorghum (kafirin) and as a minor protein, avenin in oats. They are characterised by a high glutamine and proline content and are generally soluble only in strong alcohol [70-80%] solutions, light acids, and alkaline solution. They do not coagulate in heat. They hydrolyse into prolin and ammonia. Some prolamins, notably gliadin, and similar proteins found in the tribe Triticeae (see