Purification and subunit structure of legumin of Vicia faba L. (broad bean).
Zonal isoelectric precipitation was shown to be an effective method for the preparation of legumin which was homogeneous as judged by ultracentrifugation and polyacrylamide-gel electrophoresis. The subunit structure of legumin was investigated by preparative sodium dodecyl sulphate-polyacrylamide-gel electrophoresis and ion-exchange chromatography in urea. Five distinct subunits, of which two were acidic (alpha) and had a molecular weight of 37000, and three were basic (beta) with molecular weights of 20100, 20900 and 23800, were identified. The alpha and beta subunits were present in equimolar amounts in the legumin molecule and, in view of this and molecular-weight considerations, an alpha(6)beta(6) subunit model was proposed for legumin.
D000596:Amino Acids / Q000032:analysis; D011232:Chemical Precipitation; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D008968:Molecular Conformation; D008970:Molecular Weight; D010940:Plant Proteins / Q000032:analysis / Q000302:isolation & purification*; D010944:Plants / Q000032:analysis*; D012967:Sodium Dodecyl Sulfate; D014461:Ultracentrifugation
D000596:Amino Acids; D046911:Macromolecular Substances; D010940:Plant Proteins; D012967:Sodium Dodecyl Sulfate