Wheat storage proteins

The wheat storage proteins without interchain disulfide bonds are monomeric and are termed gliadins, those with interchain disulfide bonds are polymeric and are called glutenins. Gliadins plus glutenins form gluten. Originally, it was assumed that the toxicity for CD patients was restricted to... 

Payne P.I. Genetics of wheat storage proteins and the effect of allelic variation on bread-making quality. Artnu. Rev. Plant Physiol. 38 141-153, June 1987. 

Y. Dong, X. Li and Y. Yan, Advances in Molecular Structures of Wheat Storage Proteins and Related Research Technology , Mailei Zuowu Xuebao,... 

Marchylo, B.A., Kruger, J.E., Hatcher, D.W. Quantitative reversed-phase high-performance liquid chromatographic analysis of wheat storage proteins as a potential quality prediction tool. J. Cereal Sci. 9, 113 (1989)... 

Payne, PL, Holt, L.M., Jackson, E.A., Law, C.N. Wheat storage proteins their genetics and their potential for manipulation by plant breeding. Philos. Trans. R. Soc. London Ser. B 304, 359 (1984)... 

Birzele B and Prange A (2003), Fusarium spp. and storage fungi in suboptimally stored wheat mycotoxins and influence on wheat gluten proteins. Mycotoxin Res., 19, 162-170. 

Wheat, barley Protein stability during storage, low producer price Food crops, lower yields, more difficult to transform and manipulate... 

Most of the applications of HPLC for protein analysis deal with the storage proteins in cereals (wheat, corn, rice, oat, barley) and beans (pea, soybeans). HPLC has proved useful for cultivar identihcation, protein separation, and characterization to detect adulterations (illegal addition of common wheat flour to durum wheat flour) [107]. Recently Losso et al. [146] have reported a rapid method for rice prolamin separation by perfusion chromatography on a RP POROS RH/2 column (UV detection at 230nm), sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE), and molecular size determination by MALDl-MS. DuPont et al. [147] used a combination of RP-HPLC and SDS-PAGE to determine the composition of wheat flour proteins previously fractionated by sequential extraction. 

Triboi, E., Abdad, A., Michelena, A., Lloveras, J., Ollier, J.L., and Daniel, C. 2000. Environmental effect on the quality of two wheat genotypes 1. Quantitative and qualitative variation of storage proteins. Eur J Agron 13(1) 47-64. 

Miles, M.J., Carr, H.J., McMaster, T.J., I Anson, K.J., Belton, P.S., Morris, V., Field, J.M., Shewry, P.R., Tatham, A.S. 1991. Scanning tunneling microscopy of a wheat seed storage protein reveals details of an unusual supersecondary structure. Proc Natl Acad Sci USA 88 68-71. 

Cereal prolamins, named glutenins and gliadins in wheat, secalins in rye, and horde-ins in barley, are major storage proteins of the cereal grain endosperm. These sulfur-rich proteins comprise an N-terminal domain of proline- and glutamin-rich repeats and a C-terminal domain responsible for intrachain disulfide bonds (Breiteneder and Radauer 2004). So far, y-3 hordein (Hor v 21) from barley, Sec c 20 from rye, as well as Tri a 19 and Tri a 26 from wheat are included in the IUIS allergen list. 

Gliadins are prolamins, a group of plant storage proteins with a high proline content, found in the seeds of cereal grains wheat (gliadin), barley (hordein), rye (secalin), corn (zein) and, as a minor protein, avenin in oats. 

Shewry, PR., MUes, M.J., Tatham, A.S. (1994). The prolamin storage proteins of wheat and related cereals. Progress in Biophysics and Molecular Biology, 61, 37-59. 

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