Measurements on disulphide bonds in cereal glutelins

Abstract
Cereal glutelins were divided by dilute acetic acid extraction into‘soluble’and‘insoluble’fractions. The quantities dissolved in the cases of oats and maize were negligibly small. The S.S bonds of these fractions from wheat, rye, barley, oats and maize have been amperometrically titrated after reaction with sulphite in the absence and presence of guanidine hydrochloride to give, respectively, the accessible and total S.S groups. Accessible S.S groups are believed to be mainly inter‐polypeptide chain bonds. The results imply that wheat glutenin resembles the other glutelins in being highly crosslinked. There is some evidence that the density of crosslinking is higher in oats, maize and barley glutelins, provided that the polypeptide chains of the other cereal glutelins are similar in size to those of wheat glutenin.

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