Reduction and carboxymethylation of some of the gliadin wheat proteins

Pure β-gliadin from maris widgeon wheat homogeneous on gel chromatography,disc gel electrophoresis (page) and purified on ion exchange chromatography was subjected to investigation for possible presence of intermolecular disulphide bonds. the protein was reduced by β mercaptoethanol followed by alkylation. reduced and alkylated β-gliadin was then isolated after chromatography through g-75 and g-100 sephadex gels. page electrophoresis of the two halves showed two mobility bands. the molecular weight of the proteins after reduction and alkylation was the same as the original β-gliadin before it was subjected to reduction and alkylation. it was concluded that they were not two chains of the same protein but two separate proteins.