An Improved Chromatographic Separation of Wheat Gluten Proteins

Abstract

Gel electrophoresis is at present the best procedure for the analytical fractiona-tion of wheat gluten proteins. Procedures more suitable for preparative studies, such as gel ffitration and column chromatography, have provided only partial fractionation on the basis of gel electrophoresis (Graham 1963; Lee et al. 1963; Wright, Brown, and Bell 1964). Gel electrophoretic patterns of fractions resulting from the carboxymethyl cellulose (CMC) fractionation of Simmonds and Winzor (1961) have been published by Graham (1963) and by Lee et al. (1963). These results showed that each fraction was heterogeneous, with considerable overlapping of electrophoretic bands from neighbouring fractions, and that fractions eluted late in the chromatogram were contaminated because of tailing of earlier fractions. The modification of the Simmonds and Winzor procedure described below results in an improved fractionation of gluten proteins as judged by starch-gel electrophoresis.

IgE antibodies to wheat flour components Studies with sera from subjects with bakers' asthma or coeliac condition

“…2) separates the albumins and globulins from the gliadin proteins since the latter have much lower mobilities. The glutenin protein of intermediate molecular size (Wrigley, 1965) migrates slowly as a diffuse region. which have the highest mobility for this group of proteins.…”

“…2) because of its high molecular weight, remains at the point of application. The glutenin protein of intermediate molecular size (Wrigley, 1965) migrates slowly as a diffuse region. The only cross-contamination detectable (at high loadings) in the samples examined by starch gel electrophoresis was between the albumin and gliadin preparations.…”