Glycoconjugate Journal

, Volume 14, Issue 4, pp 449–456

Isolation, characterization and molecular cloning of the bark lectins from Maackia amurensis

  • Els J.M Van Damme
  • Fred Van Leuven
  • Willy J Peumans
Article

DOI: 10.1023/A:1018595300863

Cite this article as:
Van Damme, E.J., Leuven, F.V. & Peumans, W.J. Glycoconj J (1997) 14: 449. doi:10.1023/A:1018595300863

Abstract

A detailed study was made of the bark lectins of the legume tree Maackia amurensis using a combination of protein purification and cDNA cloning. The lectins, which are the most abundant bark proteins, are a complex mixture of isoforms composed of two types of subunits of 32 and 37 kDa, respectively. Isolation and characterization of the homotetrameric isoforms indicated that the 32 kDa subunit exhibits a 100-fold stronger haemagglutinating activity than the 37 kDa subunit. Molecular cloning confirmed that the two lectin subunits are encoded by different genes. The 32 kDa subunit is apparently encoded by a single gene, whereas two highly homologous genes encode the 37 kDa subunit. A comparison of the deduced amino acid sequences of the bark lectin cDNAs and the previously described cDNA encoding the seed haemagglutinin demonstrated that they are encoded by different genes. Abbreviations: LECMAHb, cDNA clone encoding Maackia amurensis bark haemagglutinin; LECMALb, cDNA clone encoding Maackia amurensis bark leucoagglutinin; MALb, Maackia amurensis bark leucoagglutinin; MAHb, Maackia amurensis bark haemagglutinin

bark proteinsMaackia amurensiscDNA cloninglectin

Copyright information

© Chapman and Hall 1997

Authors and Affiliations

  • Els J.M Van Damme
    • 1
  • Fred Van Leuven
    • 2
  • Willy J Peumans
    • 1
  1. 1.Laboratory for Phytopathology and Plant ProtectionKatholieke Universiteit LeuvenLeuvenBelgium
  2. 2.Center for Human GeneticsKatholieke Universiteit LeuvenLeuvenBelgium