Inhibition by ricin of protein synthesis in vitro: 60 S ribosomal subunit as the target of the toxin.
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.
D000818:Animals; D002250:Carbon Radioisotopes; D006160:Guanosine Triphosphate; D066298:In Vitro Techniques; D008099:Liver / Q000166:cytology / Q000378:metabolism; D010445:Peptide Elongation Factors; D010649:Phenylalanine / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases; D037121:Plant Lectins; D010947:Plants, Toxic; D011072:Poly U / Q000378:metabolism; D014176:Protein Biosynthesis; D051381:Rats; D012270:Ribosomes / Q000187:drug effects* / Q000378:metabolism; D012276:Ricin / Q000494:pharmacology; D012278:Ricinus; D014118:Toxins, Biological / Q000494:pharmacology*
D002250:Carbon Radioisotopes; D010445:Peptide Elongation Factors; D037121:Plant Lectins; D014118:Toxins, Biological; D011072:Poly U; D010649:Phenylalanine; D006160:Guanosine Triphosphate; D012276:Ricin; D010744:Phosphoric Monoester Hydrolases