Gluten immunochemistry motif", which is found in wheat and other "Triticeae" genera.(see also: ). Alpha-2 secalin, the glutinous protein in rye, is composed of two amino-terminal overlapping T-cell sites at positions (8-19) and (13-23). Although T-cell responses to many prolamins can be found in coeliac disease, one particular gliadin, α2-gliadin appears to be the focus of T-cells. These responses were dependent on prior treatment with tissue transglutaminase. Α2-gliadin differs from the other α-gliadins, specifically because it contains an insert of 14 amino acids. This particular insertion creates 6 T-cell sites where, in the most similar gliadins, there are 2 or less sites.
Gliadin Gliadin Gliadin (a type of prolamin) is a class of proteins present in wheat and several other cereals within the grass genus "Triticum". Gliadins, which are a component of gluten, are essential for giving bread the ability to rise properly during baking. Gliadins and glutenins are the two main components of the gluten fraction of the wheat seed. This gluten is found in products such as wheat flour. Gluten is split about evenly between the gliadins and glutenins, although there are variations found in different sources. Gliadin is the water-soluble component of gluten, while glutenin is insoluble. There are three