Agarose gel filtration of Triticum vulgare proteins in dissociating solvents

Certain wheat proteins (glutenins emerged from 4% agarose columns at the void volumes even in the presence of 6 M guanidine hydrochloride, 4 M urea with or without 1% sodium dodecyl sulphate, and 8 M urea. These proteins were of considerably greater molecular size than bovine thyroglobulin (sub-unit MW 335000). Urea plus sodium dodecyl sulphate was the most effective dissociating solvent. Low MW wheat flour proteins, which had been covalently labelled with a fluorescein derivative, were not incorporated through formation of new disulphide bonds into higher MW fractions during acidic extraction of flour. Limited incorporation through non-covalent association was observed. The results do not support the contention that glutenin is an artifact of extraction. It has been confirmed that all the protein of wheat flour is not extractable with water followed by 2 M urea.