[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) x SDS-PAGE and NEPHGE(Non-Equilibrium PI-gradient Electrophoresis) x SDS-PAGE.
Deng
Z Y
ZY
Northwestern Agricultural-Forestry University of Science & Technical, Yangling Shaanxi 712100, China.
Zhao
H X
HX
Fan
S H
SH
Ji
W Q
WQ
Guo
A G
AG
Xue
X Z
XZ
D000595:Amino Acid Sequence; D015180:Electrophoresis, Gel, Two-Dimensional; D005983:Glutens / Q000031:analogs & derivatives* / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D008970:Molecular Weight; D021122:Protein Subunits
D021122:Protein Subunits; D005983:Glutens; C037302:glutenin