Cereal Chem. 76(2):261-269Three cultivars of hard red spring (HRS) wheats with identical high molecular weight (HMW) glutenin subunit composition (5+10 type, Glu-D1d) but different dough properties and breadmaking quality were used in this study. The synthesis and accumulation characteristics of different protein fractions during grain development were examined. Samples were collected at three-day intervals from anthesis to maturity between day 10 to day 37. The nonreduced SDS-extractable glutenin aggregates of developing grains were characterized by a multistacking SDS-PAGE procedure to obtain information on the size distribution and polymerization of glutenin aggregates. The HMW to low molecular weight (LMW) glutenin subunit ratio was determined for its relationship to polymerization of the various glutenin aggregates of different molecular sizes. Glutenin proteins were quantified using an imaging densitometer. In addition, albumins and globulins, αand β-gliadins, γ-gliadins, and ω-gliadins were separated by capillary zone electrophoresis. The results indicated that albumins-globulins, gliadins, and glutenins in developing grains were present at 10 days after anthesis or earlier. Albumin-globulins decreased in proportion, while gliadins increased in proportion during grain development. Polymerization of glutenin aggregates occurred 10 days after anthesis or earlier and increased significantly throughout the grain-filling period until maturity. Larger aggregates of glutenin increased in proportion, while smaller ones decreased in proportion during grain development. Ratio of polymers to monomers increased signi-1 Published with the approval