Characterization of a lectin-binding storage protein from pea (Pisum sativum).
From the storage proteins of the pea (Pisum sativum), the fraction which interacts with the pea lectin by the sugar-binding site was studied. By electrophoretical subunit patterns and other criteria, this fraction resembles the group of the 7S storage proteins (vicilins). The fraction was resolved into subunits by micropreparative SDS PAGE. The N-terminal sequences of the individual subunits were determined. Most of these are identical with published vivilin subunit sequences; therefore this lectin-binding fraction belongs to the vicilins. Selected subunits and tryptic fragments were analysed for amino-acid compositions. Though unequivocal assignments to vicilin segments were possible, significant differences could be recognized, in particular in the tryptic fragments.
Kummer
H
H
Institut für Pharmazie und Lebensmittelchemie der Universität Würzburg.
Rüdiger
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H
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000032:analysis*; D037102:Lectins / Q000302:isolation & purification* / Q000378:metabolism; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D037121:Plant Lectins; D010940:Plant Proteins; D014674:Plant Proteins, Dietary / Q000302:isolation & purification* / Q000378:metabolism; D010946:Plants, Medicinal; D055314:Seed Storage Proteins; D014357:Trypsin
D000596:Amino Acids; D002241:Carbohydrates; D037102:Lectins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D037121:Plant Lectins; D010940:Plant Proteins; D014674:Plant Proteins, Dietary; D055314:Seed Storage Proteins; C036292:pea lectin; C015575:vicilin protein, plant; D014357:Trypsin