[Purification and biochemical characterization of high-molecular-weight-glutenin subunits 14 and 15].

The high molecular weight glutenin subunits 14 and 15 were purified from cultivars of bread wheat (Triticum aestivum) Xiaoyan 6 by preparative sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) appled a new method for visualizing protein in gels. N-terminal amino acid sequences were homologous comparing with other High-Molecular-Weight glutenin subunits. The result suggested that they were basic protein analyzed by two-dimensional electrophoresis of IEF(Isoelectric Focussing) × SDS-PAGE and NEPHGE(Non- Equilibrium PI-gradient Electrophoresis) × SDS-PAGE.