In gluten

Kleberprotein, n. gluten protein, kleberreich. a. rich in gluten. 

C.W. Wrigley, H.P. Manusu, S. Paranerupasingham and F. Bekes, in Gluten 96, ed. C.W. Wrigley, published by Royal Australian Chemical Institute Melbourne, Australia. 

Fig. 1. Some fractions of wheat gluten used for the study of the deleterious action in gluten-induced enteropathy.

It is apparent that patients with gluten-induced enteropathy respond to the administration of gluten differently from other people. It is obvious from consideration of the evidence already presented that the reason for this may lie in inadequacy of the small intestinal mucosal barrier. It is clear that the intestinal mucosa or extracts of it will inactivate the deleterious agent(s) in gluten this is a thermolabile reaction, presumably enzymatic in nature. Patients with gluten-induced... 

Sensitivity to the protein gliadin, present in gluten, results in coeliac disease. 

Taylor, J. R. N. and Emmambux, M. N. (2008). Gluten-free cereal products and beverages. In "Gluten-Free Foods and Beverages from Millets", (E. K. Arendt and F. D. Bello, Eds.). Elsevier Inc. 

The gentle deamidation of gluten proteins by acetic acid resulted in minor electrophoretic changes in gluten proteins, caused by partial proteolysis, especially when... 

Li, W., Tsiami, A., Bollecker, S., Schofield, D. 2004. Glutathione and related thiol compounds. II. The importance of protein bound glutathione and related protein-bound compounds in gluten proteins. J Cereal Sci 39 213-224. 

Marsh, M.N., Morgan, S., Ensari, A., Wardle, T., Lobley, R., Mills, C., Auricchio, S. 1995. In vivo activity of peptide 31 —43,44—55,56-68 of alfa-gliadin in gluten sensitive entherop-athy (GSE). Gastroenterology 108 A871. 

Figure 6.1. The role of HMW subunits in gluten structure and functionality. Amino acid sequences derived from direct analysis of purified proteins and the isolation and sequencing of corresponding genes show that the proteins have highly conserved structures, with repetitive domains flanked by shorter nonrepetitive domains containing cysteine residues (SH) available for formation of interchain disulphide bonds. Molecular modelling indicates that the individual repetitive domains form a loose spiral structure (bottom right) while SPM shows that they interact by noncovalent forces to form fibrils (centre right). Includes figures from Parchment et al. (2001) and Humphries et al. (2000).

Malabsorption syndromes. Particularly in gluten-sensitive enteropathy and tropical sprue, poor absorption of folic acid from the small intestine often leads to a megaloblastic anaemia. 

The fingerprinting of gliadins and glutenins in various wheat flours by LC-MS shows complex traces with more than 20 peaks. The two major components, i.e., and Ys gliadin, were identified through A-terminal sequencing and accurate-mass determination [52]. The components were proposed as markers to detect traces of wheat in gluten-free food preparations. 

J. Lefebvre, Y. Popineau and M. Cornec, in Gluten Proteins, Association of Cereal Research, Detmold, 1994, pp. 180-189. 

In case of bread wheat, increases in gluten elasticity could be obtained by inserting additional genes for HMW-GS to increase the total amount of HMW subunit protein. In addition, these genes could possibly be mutated to give more subtle differences, due to effects on the cross-linking or other properties of the glutenin polymers. 

O. D. Anderson, B. Cassidy, J. Steffen, J. Dvorak, and F.C. Greene, 1991. Structure of the high-and low- molecular-weight gene families of the homoeologous group 1 chromosomes of the hexaploid bread wheat cultivar Cheyenne, pp. 512-519 in Gluten Proteins 1990. W. Bushuk and R. Tkachuk, eds. Am. Assoc. Cereal Chem. St. Paul, MN. 

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