RIBOSOME-INACTIVATING LECTINS WITH POLYNUCLEOTIDE - ADENOSINE GLYCOSIDASE ACTIVITY

Lectins from Aegopodium podagraria (APA), Bryonia dioica (BDA), Galant hus nivalis (GNA), Iris hybrid (IRA) and Sambucus nigra (SNAI), and a new lectin-related protein from Sambucus nigra (SNLRP) were studied to ascertain whether they had the properties of ribosome-inactivating pr oteins (RIP), IRA and SNLRP inhibited protein synthesis by a cell-free system and, at much higher concentrations, by cells and had polynucle otide:adenosine glycosidase activity, thus behaving like non-toxic typ e 2 (two chain) RIP, APA and SNAI had much less activity, and BDA and GNA did not inhibit protein synthesis. (C) 1997 Federation of European Biochemical Societies.