Cereal Chem 44:221 - 228.  |  VIEW ARTICLE
Isolation and Chemical Comparison of Different Gamma-Gliadins from Hard Red Winter Wheat Flour.

F. R. Huebner, J. A. Rothfus, and J. S. Wall. Copyright 1967 by the American Association of Cereal Chemists, Inc. 

By a combination of ion-exchange and gel-filtration chromatography, gamma-gliadin has been separated into three different components. Elution of gliadin from sulfoethyl cellulose (SEC) columns with a nonlinear sodium chloride gradient (0.01-0.3M) contained in 2M dimethylformamide-0.01M acetate buffer (pH 2.1) gave three peaks, each of which contained a component having a mobility in the range ascribed to gamma-gliadin on starch-gel electrophoresis. Contaminating beta-gliadins contained in two of the peaks were eliminated by subsequent chromatography on SEC in 5M urea at pH 2.5 and by gel filtration through a 200-cm. column of Sephadex G-50 in 0.05M acetic acid. The behavior of gamma-gliadin during SEC chromatography was due to heterogeneity of the protein fraction rather than to molecular aggregation. Separated gamma-gliadins migrated at slightly different rates upon electrophoresis in starch gel and differed significantly in content of lysine, tryptophan, tyrosine, phenylalanine, glutamic acid, and proline.