Cereal Chem 44:143 - 151.  |  VIEW ARTICLE
Solubilization and Fractionation of Wheat Flour Proteins Insoluble in Dilute Acetic Acid.

E. S. Inamine, E. G. Noble, and D. K. Mecham. Copyright 1967 by the American Association of Cereal Chemists, Inc. 

The gelatinous residue obtained by exhaustive extraction of flour with 0.01M acetic acid and removal of much of the starch by centrifuging appears to consist largely of protein material resembling glutenin. Treatment of the gelatinous residue with 0.1M aqueous dimethylaminoethanol solubilized about 85% of the protein; most of the accompanying carbohydrate remained insoluble. The solubilized protein then could be dissolved in 50% acetic acid-0.15M sodium chloride, or other solvents with strong protein-dissociating properties, and subjected to gel-filtration chromatography on columns of agarose or polyacrylamide beads. Two high-molecular-weight fractions were obtained. One fraction appeared in the void volume of the agarose column and, like glutenin, did not migrate into a starch gel during electrophoresis. The second fraction required further purification on polyacrylamide beads of smaller pore size. Recovered material gave a trailing pattern upon starch-gel electrophoresis that extended between the origin and a position where the gamma-gliadin band would occur under similar conditions. After the fractions were reduced and alkylated, the electrophoresis patterns were similar to those of reduced and alkylated glutenin, but a few additional faster-moving bands were present in the second fraction.