Cereal Chem 67:464-470 | VIEW
Quantitative Variation of Wheat Proteins from Grain at Different Stages of Maturity and from Different Spike Locations.
F. R. Huebner, J. Kaczkowski, and J. A. Bietz. Copyright 1990 by the American Association of Cereal Chemists, Inc.
Hard red spring wheats were grown in a greenhouse and hard red winter wheats in the field. Kernels were removed from the spring wheats periodically after flowering, and proteins analyzed by reversed-phase and size-exclusion high-performance liquid chromatography (HPLC) to reveal their compositions and rates of synthesis. Mature dried wheat kernels from the top, middle, and bottom of spikes were weighed and stored for analyses. Results revealed synthesis of both gliadin and glutenin early during maturation. HPLC patterns of gliadins (soluble in 70% ethanol) from individual kernels changed quantitatively until approximately five weeks after anthesis. Patterns also varied with spike location and kernel size. For glutenin, qualitative subunit compositions remained nearly constant during kernel development, but amounts of some subunits differed, some accumulating more rapidly than others until maturity. Synthesis of gliadin increased more rapidly than that of glutenin until the fifth week after anthesis; after this, glutenin accumulated more rapidly than gliadin. Amounts of individual high molecular weight glutenin subunits varied significantly between two varieties during maturation, suggesting differential expression of alleles at the Glu-1 loci that code these polypeptides.