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

¹Northwestern Agricultural-Forestry University of Science & Technical, Yangling Shaanxi 712100, China.

Yi Chuan Xue Bao = Acta Genetica Sinica

|February 24, 2001

Abstract:

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) x SDS-PAGE and NEPHGE(Non-Equilibrium PI-gradient Electrophoresis) x SDS-PAGE.

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