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Two-Dimensional Electrophoretic Analysis of Wheat Seed Proteins¹

High resolution two-dimenslonal (2-D) electrophoresis with isoelectric focusing in the first dimension and electrophoresis in sodium dodecyl sulfate in acrylamide gradient gels in the second dimension has been used to produce maps of proteins, including glutenins and gliadins, extracted from wheat seeds. Amino acid substitutions producing single or multiple charge changes, and additions or deletions altering protein mass by approximately 2% are visible on these gels; the former produce horizontal displacements in gel patterns, the latter vertical displacements. The thesis that mutations in storage proteins produce grid patterns of variants on 2-D gels has been examined experimentally, and confirmatory results have been obtained using 14 varieties of wheat. The results suggest that 2-D analysis will be useful for varietal identification, for classification of storage proteins of wheat, and for studies un the geneology of wheats.

Key Words: Triticum aestivum L. • Iso-Dalt • Chinese Spring • Maris Freeman • Carbamylation • Gliadins

² Program director, scientific associate, visiting scientist, and director of research, respectively.

Received for publication September 10, 1984.