Cereal Chem 62:319-326   |  VIEW ARTICLE
Two-Dimensional Fractionation of the Endosperm Proteins of Bread Wheat (Triticum aestivum): Biochemical and Genetic Studies.

P. I. Payne, L. M. Holt, M. G. Jarvis, and E. A. Jackson. Copyright 1985 by the American Association of Cereal Chemists, Inc. 

Wheat endosperm protein, extracted in the presence of 2-mercaptoethanol and sodium dodecyl sulfate, fractionated into about 100 components of molecular weight greater than 25,000 by two-dimensional polyacrylamide gel electrophoresis under dissociating conditions. These components were grouped into high molecular weight glutenin subunits, low molecular weight glutenin subunits (two groups), gliadins, high molecular weight albumins, globulins, nonstorage proteins, and triplet-band subunits (two groups). The triplet-band proteins were very recently discovered by electrophoresis under nonreducing conditions. The chromosome and chromosome-arm location of most components was determined using genetic lines of Chinese Spring. A minor, basic protein of molecular weight similar to gliadins and low molecular weight glutenin subunits was shown to be controlled by genes on the long (L) arm, rather than the short arm, of chromosome 1A. It only occurred in those varieties which lacked a 1AL-encoded high molecular weight subunit of glutenin. The possible effects on breadmaking quality of non-prolamin type storage proteins are discussed.