Inhibition by ricin of protein synthesis in vitro. Inhibition of the binding of elongation factor 2 and of adenosine diphosphate-ribosylated elongation factor 2 to ribosomes.
The binding of EF2 (elongation factor 2) and of ADP-ribosyl-EF 2 to rat liver ribosomes is inhibited by ricin. This result suggests that the native enzyme and its ADP-ribose derivative have the same or closely related binding sites on the ribosome. The inhibition by ricin of the binding of EF 2 to ribosomes is consistent with the previous observation that ricin affects EF 2-catalysed translocation during polypeptide chain elongation.
D000244:Adenosine Diphosphate / Q000378:metabolism; D000818:Animals; D066298:In Vitro Techniques; D008099:Liver / Q000187:drug effects; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D010445:Peptide Elongation Factors / Q000037:antagonists & inhibitors*; D010940:Plant Proteins / Q000494:pharmacology*; D011485:Protein Binding; D014176:Protein Biosynthesis; D051381:Rats; D012266:Ribose / Q000378:metabolism; D012270:Ribosomes / Q000187:drug effects* / Q000378:metabolism; D012276:Ricin / Q000494:pharmacology*
D010445:Peptide Elongation Factors; D010940:Plant Proteins; D009243:NAD; D000244:Adenosine Diphosphate; D012266:Ribose; D012276:Ricin