Prolamin cereal

Prolamines. Proteins insoluble in water, but dissolving in aqueous alcohol solutions. Found in the seeds of cereals. 

Cereal proteins when classified by the Osborne sequential extraction method yield four different classes albumins, which are water soluble, globulins, which are soluble in salt solutions, prolamins, which are soluble in alcohol-water mixtures, and glutelins, which are soluble in dilute acid or alkali. Chen and Bushuk added a fifth fraction by dividing the glutelin into two fractions, one soluble in dilute (0.05 m) acetic acid and the other insoluble in this reagent.5... 

These organelles occur in the endosperm of cereal grains and their structures are tissue specific. They are about 2-5 im in diameter and often contain globoid and occasionally crystalloid inclusions. Prolamin accumulates in small or large spherical bodies. Crystalline protein bodies are the sites of accumulation of nonprolamin storage proteins. 

Cornell, H. J., McLachlan, A., and Cullis, P. G. (2002). Extraction of cereal prolamins and their toxicity in coeliac disease. ]. Biochem. Mol. Biol. Biophys. 6,151-158. 

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. 

GL Lookhart, LD Albers. Correlations between reversed-phase high-performance liquid chromatography and acid- and sodium dodecyl sulfate-polyacrylamide gel electrophoretic data on prolamines from wheat sister lines differing widely in baking quality. Cereal Chem 65 222-227, 1988. 

GL Lookhart, Y Pomeranz. Characterization of oat species by polyacrylamide gel electrophoresis and high performance liquid chromatography of their prolamin proteins. Cereal Chem 62 162-166, 1985. 

GL Lookhart. Identification of oat cultivars by fingerprinting their prolamin fractions via polyacrylamide gel electrophoresis (PAGE) and reversed phase-high performance liquid chromatography (RP-HPLC). Cereal Foods World 29 507, 1984. 

WDEIA is a serious affection where symptoms are not only connected to wheat protein consumption, but they also appear after the introduction of wheat proteins into the digestive track, and following physical effort. Research on IgE of patients suffering from WDEIA showed that wheat gliadins are responsible for the disease, as well as corresponding taxonomic prolamines of closely related cereals (Varjonen et al., 1997). 

Simpson, D.J. 2001. Proteolytic degradation of cereal prolamins—The problem with proline. Plant Sci 161 825-838. 

Skerritt, J.H., Hill, A.S., Andrews, J.L. 2000. Antigenicity of wheat prolamins Detailed epitope analysis using a panel of monoclonal antibodies. J Cereal Sci 32 259-279. 

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. 

Shewry PR, Tatham AS. The prolamin storage proteins of cereal seeds Structure and evolution. Biochem J 1990 267 1-12. 

In genetically susceptible individuals, ingestion of cereal prolamins from wheat, barley, rye, and possibly oats initiates an inflammatory disorder during which the small intestinal mucosa is damaged. This process is accompanied by malabsorption, activation of the intestinal immune system, and... 

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, P.R. and Tatham, A.S. (1990). The prolamins storage proteins of cereal seeds— structure and evolution. Biochem. J., 267, 1-12. 

Nonwater (gluten) and alcohol-soluble (prolamin) fractions from cereal proteins... 

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. 

Lysine is the first nutritionally limiting essential amino acid in most cereals (1.5-4%) tryptophan (0.8-2%) is the second limiting amino acid in maize, and threonine (2.7-3.9%) in other cereals. The high content of prolamins in cereals is responsible for the low content of essential amino acids like lysine, threonine, valine and isoleucine. Rice and oats have a better balance of essential amino acids than other cereals due to a lower content of prolamins. 

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