| Gliadin/LMW glutenin | |
|---|---|
| Identifiers | |
| Symbol | Glia_glutenin |
| InterPro | IPR001954 |
| Gliadin [Seed storage proteins] N-terminal helical domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Gliadin | ||||||||
| Pfam | PF13016 | ||||||||
| InterPro | IPR016140 | ||||||||
| |||||||||
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.
Both gliadins and glutenins are not water-soluble, but gliadins are soluble in 70% aqueous ethanol.[1] There are three main types of gliadin (α, γ, and ω), to which the body is intolerant in coeliac (or celiac) disease. Diagnosis of this disease has recently been improving.
Gliadin can cross the intestinal epithelium. Breast milk of healthy human mothers who eat gluten-containing foods presents high levels of non-degraded gliadin.[2][3]
- ^ Ribeiro M, Nunes-Miranda JD, Branlard G, Carrillo JM, Rodriguez-Quijano M, Igrejas G (November 2013). "One hundred years of grain omics: identifying the glutens that feed the world". Journal of Proteome Research. 12 (11): 4702–16. doi:10.1021/pr400663t. PMID 24032428.
- ^ Bethune MT, Khosla C (February 2008). "Parallels between pathogens and gluten peptides in celiac sprue". PLOS Pathogens. 4 (2): e34. doi:10.1371/journal.ppat.0040034. PMC 2323203. PMID 18425213.
- ^ Chirdo FG, Rumbo M, Añón MC, Fossati CA (November 1998). "Presence of high levels of non-degraded gliadin in breast milk from healthy mothers". Scandinavian Journal of Gastroenterology. 33 (11): 1186–92. doi:10.1080/00365529850172557. PMID 9867098.