Ribosome-inactivating lectins with polynucleotide:adenosine glycosidase activity.
Lectins from Aegopodium podagraria (APA), Bryonia dioica (BDA), Galanthus 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 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 SNAI had much less activity, and BDA and GNA did not inhibit protein synthesis.
Battelli
M G
MG
Dipartimento di Patologia sperimentale dell'Università di Bologna, Italy.
Barbieri
L
L
Bolognesi
A
A
Buonamici
L
L
Valbonesi
P
P
Polito
L
L
Van Damme
E J
EJ
Peumans
W J
WJ
Stirpe
F
F
D016475:3T3 Cells; D000818:Animals; D002460:Cell Line; D002474:Cell-Free System; D027801:Galanthus; D006367:HeLa Cells; D006801:Humans; D007700:Kinetics; D037102:Lectins / Q000378:metabolism* / Q000494:pharmacology; D051379:Mice; D037121:Plant Lectins; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology*; D054788:Ribosome Inactivating Proteins; D012270:Ribosomes / Q000378:metabolism*
D037102:Lectins; D037121:Plant Lectins; D011500:Protein Synthesis Inhibitors; C050600:Sambucus nigra lectins; D054788:Ribosome Inactivating Proteins