Isolation and characterization of a minor legumin and its constituent polypeptides from Pisum sativum (pea).
The purification and characterization of a minor legumin species from Pisum sativum is described. Electrophoretic data indicate that it corresponds to a legumin subunit pair previously designated L1. The beta-polypeptides of the minor legumin have a phenylalanine N-terminus. This is the first time that an amino acid other than glycine has been reported as the N-terminus of the basic polypeptides from legumin-like proteins from any plant species. Sequence analyses of the isolated alpha- and beta-polypeptides of the minor legumin show that it does not correspond to any of the three legumin gene families that have previously been defined on the basis of DNA hybridizations and genetic analyses.
March
J F
JF
John Innes Institute, Norwich, U.K.
Pappin
D J
DJ
Casey
R
R
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000032:analysis*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis*; D010940:Plant Proteins; D014674:Plant Proteins, Dietary / Q000302:isolation & purification*; D010946:Plants, Medicinal; D000097793:Legumins
D010446:Peptide Fragments; D010940:Plant Proteins; D014674:Plant Proteins, Dietary; D000097793:Legumins