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Ribosome‐inactivating lectins with polynucleotide:adenosine glycosidase activity
Author(s) -
Battelli Maria Giulia,
Barbieri Luigi,
Bolognesi Andrea,
Valbonesi Paola,
Polito Letizia,
Van Damme Els J.M,
Peumans Willy J,
Stirpe Fiorenzo
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00463-8
Subject(s) - ribosome inactivating protein , sambucus nigra , lectin , biochemistry , glycoside hydrolase , polynucleotide , ribosome , chemistry , biology , enzyme , rna , gene
Lectins from Aegopodium podagraria (APA), Bryonia 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.