Glutenin subunits

Various new methods such as capillary electrophoresis and reversed-phase HPLC have been used to characterise glutenin subunits. These... 

Dewar, D. H., Amato, M., Ellis, H. J., Pollock, E. L., Gonzalez-Cinca, N., Wieser, H., and Ciclitira, P. J. (2006). The toxicity of high molecular weight glutenin subunits of wheat to patients with coeliac disease. Eur. ]. Gastroenterol. Hepatol. 18, 483-491. 

Figure 5. SDS-PAGE of alkylated glutenin subunits of bread wheat fractionated by gel filtration on Sephadex G-200...

It has been shown (36) that the genes for the key glutenin subunits are located on the long arm of the ID chromosome. 

Halford, N.G., Field, J.M., Blair, H., Urwin, P., Moore, K., Robert, L., Thompson, R., Havell, R.B., Tatham, A.S., and Shewry, P.R. (1992). Analysis of the HMW glutenin subunits encoded by chromosome lA of bread wheat (Tritkum aestimm L.) indicates quantitative effects on grain quaUty. Theor. Appl. Genet., 83, 373-378. 

Kasarda, D.D., King, G., and Kumonsinski, T.F. (1994). Comparison of p-spiral structures in wheat high molecular weight glutenin subunits and elastin by molecular modelling. In ... 

Payne, P.I., Nightingale, M.A., Krattinger, A.F., and Holt, L.M. (1987). The relationship between HMW glutenin subunit composition and the bread-making quality of British grown... 

Tao, H.P., Adalsteins, A.E., and Kasarda, D.D. (1992). Intermolecular disulfide bonds hnk specific high molecular weight glutenin subunits in wheat endosperm. Biochim. Biophys. Acta, 1159, 13-21. 

Vawser, M.J. and Cornish, G.B. (2004). Over-expression of HMW glutenin subunit Glu-Bl lx in hexaploid wheat varieties (Triticum aestivumh.). Aust. J. Agric. ScL, 55, 577-588. 

Figure 20.7. Structure of HMW glutenin subunit showing (a) branching (b) spiral structure by Atomic Force Microscopy (AFM). (From Humphries et al. (2000), Cereal Chem. 77, 107-110.)...

Heterogeneity of Genes Encoding the Low Molecular Weight Glutenin Subunits of Bread Wheat... 

The sulfur-rich prolamins are quantitatively the most abundant group in wheat, barley and rye, accounting for approximately 80-90% of total prolamin fractions. They include polymeric and monomeric components and consist of at two families in each species, the B- and y-hordeins of barley two types of y-secalin of rye and a, 3 and y-gliadins and LMW glutenin subunits of wheat. The sulfur-poor prolamins include C-hordeins of barley, (O-secalin of rye and co-gliadin of wheat. 

Figure 13.10 SDS-PAGE of seed storage proteins of T. aestivum L., cv S. ranozreika 2 and their mutant forms. Lane 1- control of T. aestivum, 2,4,5, 6, and 7 are lanes of mutant forms type sphaerococcum. The HMW-glutenin subunits are with high weight (more than 160,000), and well separated from other prolamins [13].

Figure 13.11 SDS-PAGE of polymeric protein (after reduction to subunits). Group A HMW glutenin subunits showing x- and y-type subunits. Group B-, C-, D- LMW glutenin subunits. Arrow indicates subunit D [41].

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