Abstract
Poly(U)-directed polyphenylalanine synthesis by rat liver ribosomes is strongly inhibited by ricin. Experiments involving hybridization between subunits derived from normal and ricin-treated ribosomes demonstrate that the 60S subunit is the site of action of the toxin. The toxin inactivates the 60S subunit independently of the presence of the 40S subunit.
MeSH Terms
Animals
Carbon Radioisotopes
Guanosine Triphosphate
In Vitro Techniques
Liver/cytology,metabolism
Peptide Elongation Factors
Phenylalanine/metabolism
Phosphoric Monoester Hydrolases
Plant Lectins
Plants, Toxic
Poly U/metabolism
Protein Biosynthesis
Rats
Ribosomes/drug effects,metabolism
Ricin/pharmacology
Ricinus
Toxins, Biological/pharmacology
Chemicals
Carbon Radioisotopes
Peptide Elongation Factors
Plant Lectins
Toxins, Biological
Poly U
Phenylalanine
Guanosine Triphosphate
Ricin
Phosphoric Monoester Hydrolases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Sperti S
Montanaro L
Mattioli A
Stirpe F
References (11)
11 references, click to expand
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