Pea (Pisum sativum L.) seed isolectins 1 and 2 and pea root lectin result from carboxypeptidase-like processing of a single gene product

@article{Hoedemaeker2004PeaS,
  title={Pea (Pisum sativum L.) seed isolectins 1 and 2 and pea root lectin result from carboxypeptidase-like processing of a single gene product},
  author={F. J. Hoedemaeker and Michael Richardson and C. D{\'i}az and B. D. S. Pater and J. Kijne},
  journal={Plant Molecular Biology},
  year={2004},
  volume={24},
  pages={75-81}
}
  • F. J. Hoedemaeker, Michael Richardson, +2 authors J. Kijne
  • Published 2004
  • Biology, Medicine
  • Plant Molecular Biology
  • The complete amino acid sequences of the α-subunits of pea (Pisum sativum L.) seed and root lectin, the C-terminal amino acids of the β-subunits of pea seed lectin, and most of the sequence of the β-subunit of pea root lectin were determined. In contrast to earlier reports it was shown that the β-subunits of both seed isolectins end at Asn-181. The α1 subunits end at Gln-241 (major fraction) or Lys-240 (minor fraction), whereas the α2 subunits end at Ser-239, Ser-238, Ser-237 or Thr-236. psl… CONTINUE READING
    Proline specific peptidases.
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    Root Lectins and Rhizobia
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    • PDF

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