THE SEPARATION OF THE PROTEINS OF WHEAT BY ACRYLAMIDE GEL ELECTROPHORESIS, WITH SPECIAL REFERENCE TO MOTTLED AND UNMOTTLED WHEAT

Abstract

The proteins of wheat grains were studied by the technique of acrylamide gel electrophoresis. This study provided the opportunity to show the effects, on the proteins resolved by these methods, of different factors and variables. These include some items of technique, effects due to the variety to which the grains belong and to the condition known as mottling, and some correlations with the morphology of the grain and with changes that accompany germination. Albumins and globulins were extracted from whole ungerminated mottled and unmottled wheat grains (var. Festival), from embryos of mottled and unmottled grain, and from the various parts of grain germinated for 2, 4, and 6 days under defined conditions. The extracted proteins were separated on [Formula: see text] acrylamide gels at pH 8.3. Glutens were extracted from the same materials and were separated on [Formula: see text] acrylamide gels at pH 5.0; some were separated at pH 4.5 also. The albumins and globulins and glutens of the whole ungerminated grain of three varieties of mottled and unmottled wheat are described and differences due to variety and mottling are discussed. The protein patterns of whole grain, dominated by endosperm, were remarkably constant though varietal effects were seen. Albumin and globulin and gluten fractions each had characteristic patterns but the observed differences between mottled and unmottled grain were quantitative, not qualitative. Proteins of embryos differed from those of endosperm and upon germination complementary changes in endosperm and embryo (roots and shoots) proteins could be observed.