Ribosome-inactivating lectins with polynucleotide:adenosine glycosidase activity
- Battelli M. G.
- Barbieri L.
- Bolognesi A.
- Buonamici L.
- Valbonesi P.
- Polito L.
- Van Damme E. J. M.
- Peumans W. J.
- Stirpe F.
Publication date
January 1997
DOIAbstract
Lectins from Aegopodium podagraria (APA), Bryonin dioica (BDA), Galanthus nivalis (GNA), Iris hybrid (IRA) and Sambucus nigra (SNAl), and a new lectin-related protein from Sambucus nigra (SNLRP) were studied to ascertain whether they had the properties of ribosome-inactivating proteins (RIP). IRA and SNLRP inhibited protein synthesis by a cell-free system and, at much higher concentrations, by cells and had polynucleotide:adenosine glycosidase activity, thus behaving like non-toxic type 2 (two chain) RIP. APA and SNAl had much less activity, and BDA and GNA did not inhibit protein synthesis
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