A comparison of the fine saccharide-binding specificity of Dioclea grandiflora lectin and concanavalin A.

@article{Gupta1996ACO,
  title={A comparison of the fine saccharide-binding specificity of Dioclea grandiflora lectin and concanavalin A.},
  author={Dwijendra Gupta and Stefan Oscarson and T Shantha Raju and Paula Stanley and Eric J. Toone and Curtis Brewer},
  journal={European journal of biochemistry},
  year={1996},
  volume={242 2},
  pages={320-6}
}
The lectin from the seeds of Dioclea grandiflora (DGL) is a Man/Glc-specific tetrameric protein with physical and saccharide-binding properties reported to be similar to that of the jack bean lectin concanavalin A (ConA). Unlike other plant lectins, both DGL and ConA bind with high affinity to the core trimannoside moiety, 3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside, which is present in all asparagine-linked carbohydrates. In the present study, hemagglutination inhibition… CONTINUE READING
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