Homoeologous chromosomal location of the genes encoding thionins in wheat and rye

Thionins are high sulphur basic polypeptides present in the endosperm of Gramineae. In wheat there are three thionins encoded by genes located in the long arms of chromosomes 1A, 1B and 1D. Rye has one thionin encoded by a gene which has been assigned to chromosome 1R after analysis of the Imperial-Chinese Spring rye-wheat disomic addition lines. Commercial varieties and experimental stocks with a 1B/1R substitution carry the thionin from rye ( R) instead of the B thionin from wheat. The R thionin gene is not located in the large chromosomal segment representing most of the short arm of chromosome 1R

Role of the NADP/thioredoxin system in the reduction of alpha-amylase and trypsin inhibitor proteins

International audienc

Thioredoxin-linked mitigation of allergic responses to wheat

Thioredoxin, a ubiquitous 12-kDa regulatory disulfide protein, was found to reduce disulfide bonds of allergens (convert S—S to 2 SH) and thereby mitigate the allergenicity of commercial wheat preparations. Allergenic strength was determined by skin tests with a canine model for food allergy. Statistically significant mitigation was observed with 15 of 16 wheat-sensitive animals. The allergenicity of the protein fractions extracted from wheat flour with the indicated solvent was also assessed: the gliadins (ethanol) were the strongest allergens, followed by glutenins (acetic acid), albumins (water), and globulins (salt water). Of the gliadins, the α and β fractions were most potent, followed by the γ and ω types. Thioredoxin mitigated the allergenicity associated with the major protein fractions—i.e, the gliadins (including the α, β, and γ types) and the glutenins—but gave less consistent results with the minor fractions, the albumins and globulins. In all cases, mitigation was specific to thioredoxin that had been reduced either enzymically by NADPH and NADP–thioredoxin reductase or chemically by dithiothreitol; reduced glutathione was without significant effect. As in previous studies, thioredoxin was particularly effective in the reduction of intramolecular (intrachain) disulfide bonds. The present results demonstrate that the reduction of these disulfide bonds is accompanied by a statistically significant decrease in allergenicity of the active proteins. This decrease occurs alongside the changes identified previously—i.e., increased susceptibility to proteolysis and heat, and altered biochemical activity. The findings open the door to the testing of the thioredoxin system in the production of hypoallergenic, more-digestible foods