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.
Battelli M.G., Barbieri L., Bolognesi A., Buonamici L., Valbonesi P., Polito L., et al. (1997). Ribosome-inactivating lectins with polynucleotide:adenosine glycosidase activity. FEBS LETTERS, 408(3), 355-359 [10.1016/S0014-5793(97)00463-8].
Ribosome-inactivating lectins with polynucleotide:adenosine glycosidase activity
Battelli M. G.;Barbieri L.;Bolognesi A.;Buonamici L.;Valbonesi P.;Polito L.;Stirpe F.
1997
Abstract
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
