Cereal Chem 53:180 - 189.  |  VIEW ARTICLE
Properties of Wheat Gliadins Separated by Gel Filtration.

K. R. Preston and W. Woodbury. Copyright 1976 by the American Association of Cereal Chemists, Inc. 

Gliadins isolated from three hexaploid and one tetraploid wheat variety were fractionated on Sephadex G- 100 in a dissociating solvent. Four fractions of average molecular weights (mol wt) greater than 100,000 and of 44,000, 27,000 and 10,000 were obtained from each variety. Significant varietal variation in the mol wt distribution of fractions was found. The first three fractions of each variety had amino acid compositions similar to whole gliadin but the fourth fraction had an amino acid content similar to wheat albumin. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis showed that the hexaploid varieties had major subunits of mol wt 36,000, 40,000, and 50,000 and minor subunits of mol wt 10,000, 53,000, 78,000, 82,000, 88,000, 108,000, 120,000, and 130,000. The tetraploid variety lacked minor subunits of mol wt 88,000, 120,000, and 130,000. Comparison of reduced and nonreduced fractions indicated that the three lower mol wt fractions were composed of single-chain proteins. The nonreduced high-mol wt fractions gave a large number of bands of apparent mol wt 150,000-300,000, but upon reduction gave three subunits of mol wt 40,000, 50,000, and 53,000.