Plant Molecular Biology

, Volume 17, Issue 1, pp 89–100 | Cite as

Pea lectin is correctly processed, stable and active in leaves of transgenic potato plants

  • Glyn A. Edwards
  • Andrew Hepher
  • Stephen P. Clerk
  • Donald Boulter


A gene encoding the preproprotein of the pea (Pisum sativum) lectin was expressed in transgenic potato plants using a cauliflower mosaic virus (CaMV) 35S promoter or a tobacco ribulose bisphosphate carboxylase small subunit (ssRubisco) promoter. Presence of the pea lectin to levels greater than 1% of total soluble leaf protein was detected by radioimmunoassay (RIA). The pattern of expression derived from the two promoters was established using both RIA and a squash-blot immunolocalisation technique. Western blotting demonstrated that the preproprotein was correctly processed, generating α and β subunits that assembled to give an isolectin form observed in pea seeds and roots. It was also found that the haemagglutination activity and specificity of pea lectin synthesised in transgenic potato leaves was comparable to purified lectin from pea cotyledons.

Key words

Agrobacterium haemagglutination lectin (Pisumprotein processing transgenic potato 


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Copyright information

© Kluwer Academic Publishers 1991

Authors and Affiliations

  • Glyn A. Edwards
    • 1
  • Andrew Hepher
    • 2
  • Stephen P. Clerk
    • 2
  • Donald Boulter
    • 1
  1. 1.Department of Biological ScienceDurham UniversityDurhamUK
  2. 2.Shell Research Ltd.Sittingbourne Research CentreSittingbourneUK

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