Ribosome-inactivating proteins and other lectins from Adenia (Passifloraceae)
Autor: | Chiara Lubelli, Letizia Polito, Luigi Barbieri, Andrea Bolognesi, Emanuele Pelosi, Fiorenzo Stirpe |
---|---|
Přispěvatelé: | PELOSI E., LUBELLI C., POLITO L., BARBIERI L., BOLOGNESI A., STIRPE F. |
Jazyk: | angličtina |
Rok vydání: | 2005 |
Předmět: |
Adenia
TOXIN Toxicology Ribosome Chromatography Affinity Cell Line HeLa Species Specificity Reticulocyte Affinity chromatography RIBOSOME-INACTIVATING PROTEIN medicine Protein biosynthesis Animals Humans Passifloraceae Chromatography High Pressure Liquid Toxins Biological Protein Synthesis Inhibitors biology Ribosome-inactivating protein Lectin LECTIN ADENINE POLYNUCLEOTIDE GLYCOSYLASE Cytotoxicity Tests Immunologic biology.organism_classification Molecular biology Plants Toxic medicine.anatomical_structure Biochemistry biology.protein Electrophoresis Polyacrylamide Gel Rabbits Plant Lectins Ribosomes |
Popis: | The caudices of ten Adenia species contain galactose-binding lectins that were purified by affinity chromatography. All lectins but three agglutinate human erythrocytes. Six lectins consist of two unequal chains, which can be separated by reduction, and inhibit protein synthesis both by a rabbit reticulocyte lysate and by HeLa and Raji cells. The lectins from A. goetzii, A. lanceolata and A. stenodactyla had the highest cytotoxicity, inhibiting cell protein synthesis with IC50’s (concentration inhibiting by 50%) below 0.1 ng/ml, and deadenylate DNA, thus being type 2 ribosome-inactivating proteins. |
Databáze: | OpenAIRE |
Externí odkaz: |