Cereal Chem 45:413 - 420.  |  VIEW ARTICLE
Chromatography of Proteins from Wheat Gluten on Polyacrylamide Gel.

M. J. A. Crow and J. A. Rothfus. Copyright 1968 by the American Association of Cereal Chemists, Inc. 

Glutenin and gliadin fractions from wheat flour and cyanoethylglutenin (CN-Glutenin) were chromatographed on polyacrylamide gel in 8M urea. Glutenin emerged continuously over a range of Rf values from 1.0 to 0.5, consistent with the concept that glutenin is a mixture of materials which have different molecular weights. Examination of reduced and cyanoethylated fractions from glutenin by starch- gel electrophoresis disclosed a deficiency of slow-moving electrophoretic components in fractions containing materials of low molecular weight. CN-glutenin was separated into three fractions, each of which contained a different mixture of proteins. Comparison of elution patterns for CN-glutenin and gliadin showed that portions of CN-glutenin migrated as particles with apparent molecular weights near 100,000 and 40,000. The heavier fraction contained the major electrophoretic components in CN-glutenin; the lighter, fewer components that migrated slowly upon electrophoresis. Chromatography of the viscous solutions of wheat gluten proteins was facilitated by use of glass beads as support for the polyacrylamide gel.