Gliadins

In contrast, the glutenins form large polymeric structures as a result of inter-molecular disulfide bonds. 

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Elmoijani, K., Thievin, M., Michon, T., Popineau, Y., HaUet, J.N., and Gueguen, J., Synthetic genes specifying periodic polymers modelled on the repetitive domain of wheat gliadins Conception and expression, Biochem. Biophys. Res. Commun., 239(1), 240-246, 1997. 

Beyer K, Chung D. Schulz G. Mishoe M. Niggemann B, Wahn U, Sampson HA The role of wheat omega-5 gliadin IgE antibodies as a diagnostic tool for wheat allergy in childhood. J Allergy Clin Immunol 2008 122 419-421. 

De Stefano, D., Maturi, M.C., Simeon, V. et al. 2007. Lycopene, quercetin and tyrosol prevent macrophage activation induced by gliadin and IFN-gamma. Eur J Pharmacol 566 192-199. 

Fig. 10. Backscattered Raman and ROA spectra in H2O of wheat glutenin T-A-l peptide (top pair) at pH 3.5, wheat A-gliadin (middle pair) at pH 3.5, and wheat ogliadin (bottom pair) at pH 2.6. 

This chapter has reviewed the application of ROA to studies of unfolded proteins, an area of much current interest central to fundamental protein science and also to practical problems in areas as diverse as medicine and food science. Because the many discrete structure-sensitive bands present in protein ROA spectra, the technique provides a fresh perspective on the structure and behavior of unfolded proteins, and of unfolded sequences in proteins such as A-gliadin and prions which contain distinct structured and unstructured domains. It also provides new insight into the complexity of order in molten globule and reduced protein states, and of the more mobile sequences in fully folded proteins such as /1-lactoglobulin. With the promise of commercial ROA instruments becoming available in the near future, ROA should find many applications in protein science. Since many gene sequences code for natively unfolded proteins in addition to those coding for proteins with well-defined tertiary folds, both of which are equally accessible to ROA studies, ROA should find wide application in structural proteomics. 

Other workers used 0.1 m acetic acid for gluten separation then changed to dilute hydrochloric acid followed by neutralisation with sodium hydroxide.8 Byers et al. used 50% propan-l-ol in preference to 70% ethanol.9 Methods based on extraction with sodium dodecyl sulfate (SDS) have been developed by Danno10 as well as Graveland et al.11,12 Sonication of the SDS extract was introduced by Singh et al.13,14 Burnouf et al. introduced the use of dimethyl sulfoxide (DMSO) to remove monomeric proteins and a few small gliadins.15... 

Gliadins, unlike glutenins, contribute to the viscosity and the extensibility of the gluten and not its strength. 

Gluten is a mixture of proteins that can be classified as glutenins and gliadins. Extensibility is provided by glutenins while the gliadins contribute elasticity and cohesiveness. 

Coeliac disease, which is an allergy to gluten (specifically the gliadin fraction), is a cell-mediated food allergy. 

Berger (B8, B9) showed that both normal and celiac children form antibodies to a number of food proteins. These antibodies did not cause any deleterious effect in most of these individuals, but it is claimed that they have a different form in celiac children, in whom some antigens may assume a damaging role. In the celiac child certain cereals such as wheat gliadin have been shown to cause a reduction in... 

Vasomotor changes also occur when gluten is reintroduced. The patient may feel hot, show flushing or pallor, or have attacks of sweating. These have been reported by a number of observers (H8, K5, K8, W5). Detailed studies on the precise nature and/or cause of these vasomotor effects do not appear to have been carried out. They have sometimes been referred to as gliadin shock. They might repay further study. 

C5. Chaptal, J., Jean, R., Dossa, D., Bonnet, H., Paulet, A. Crastes de, and Navarro, M, Coeliac disease with intolerance of the gliadin of wheat and oats and of milk products. P6diatrie 12, 737-747 (1957). 

G4. Gerrard, J. W., Marko, A. M., and Buchan, D., Glutamic acid derivatives in juvenile and adult celiac disease, 1. Plasma glutamic acid levels after a gliadin tolerance test. Can. Med. Assoc. J. 83, 1321-1323 (1960). 

K6. Krainick, H. G., The injurious effect of gliadin in celiac disease and its probable causes. Neue Forsch. Getreideeiweiss, GetreidestUrke u. Getreideenzyme, Ber. Getreidechemiker-Tagung, Detmold 1958 120-131 (Pub. 1959) Chem. Abstr. 54, 2552c (1960). 

K8. Krainick, H. G., Debatin, F., Gautier, E., Tobler, R., and Velasco, J. A., Additional research on the injurious effect of wheat flour in celiac disease. I. Acute gliadin reaction (gliadin shock). Helv. Paediat. Acta 13, 432-454 (1958). 

V7. Visakorpi, J. K., Gliadin tolerance test its applicability to the determination of gliadin sensitivity in coeliac patients. Ann. Paediat. Fenniae 5, 67-73 (1959). 

About seventy per cent of the total nitrogen in gliadin, eight per cent in edestin and one hundred per cent in zein does not add hydrogen chloride stoichiometrically. 

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