ABSTRACT
The protein content of wheat varies between 8 and 14% on the average. Most of the protein is in the endosperm, the part that is milled into wheat flour. Gluten constitutes 90% of the endosperm proteins. Gluten itself consists roughly of equal parts of gliadin and glutenin. Gluten can be solubilized in diluted acids (formic, acetic, lactic) to an opalescent liquid that is not stable and can be partially centrifuged down. As already stated by Wieser et al., there are a number of identical structures in prolamins of other cereals also. Kasarda et al. The development of gluten-free products from wheat requires a method of analysis for prolamins. One of the methods used to analyze prolamins in raw materials or foodstuffs is electrophoresis. The first immunological methods used for the detection of prolamins were based on the Ouchterlony technique. Ciclitira et al. suggested a relationship between the antigenic structure of cereal proteins and their toxicity in celiac disease.
