Application of high-performance liquid chromatography to the assessment of subunit heterogeneity in plant 11S storage globulins.
Plant 11S storage proteins from a wide range of species have been resolved into their component subunits by ion-exchange fast protein liquid chromatography under denaturing conditions. The complex profiles obtained were reproducible and characteristic for each plant species analysed. The technique is shown to have distinct advantages over the more conventional electrophoretic approaches used to assess 11S subunit heterogeneity. The potential for the fast protein liquid chromatographic method as a simple screening system is discussed.
Lambert
N
N
AFRC Institute of Food Research, Norwich Laboratory, U.K.
Plumb
G W
GW
Wright
D J
DJ
D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005916:Globulins / Q000032:analysis*; D007202:Indicators and Reagents; D007525:Isoelectric Focusing; D010940:Plant Proteins / Q000032:analysis*; D012967:Sodium Dodecyl Sulfate
D005916:Globulins; D007202:Indicators and Reagents; D010940:Plant Proteins; D012967:Sodium Dodecyl Sulfate