Cereal Chem 66:256-262 | VIEW
Polyacrylamide Gel Electrophoresis and High-Performance Liquid Chromatography Patterns of Gliadins from Wheat Sections and Milled and Air-Classified Fractions.
G. L. Lookhart, M. Menkovska, and Y. Pomeranz. Copyright 1989 by the American Association of Cereal Chemists, Inc.
Gliadins were extracted from hard red winter wheat samples, cultivar Vona, that ranged in protein contents from 9.5 to 14.8%; from laboratory-milled and hand-dissected fractions from the hard red winter wheat; and from air-classified flours from a commercial blend of wheat flours. The gliadin extracts were obtained both from bulk wheat samples and from individual kernels. The gliadin fractions were analyzed by polyacrylamide gel electrophoresis (PAGE) and high-performance liquid chromatography (HPLC). Extract aliquots were analyzed (by PAGE and HPLC) both on a constant sample weight and constant sample protein basis. In evaluating the electrophoregrams and elution patterns, relative PAGE band intensities and HPLC elution peaks and their ratios were studied. Small differences in the gliadin PAGE and HPLC patterns were found in flour mill stream fractions and by-products of a single wheat variety, Vona, and in air-classified wheat flour fractions with wide variations in wheat protein (bulk samples). Considerable differences in PAGE and HPLC patterns were found in hand-dissected fractions. Qualitative and quantitative variations in PAGE and HPLC patterns were observed among single kernels of this wheat cultivar, which indicates gliadin heterogeneity (biotypes).