1. Inhibition of Escherichia coli protein synthesis by a limited tryptic digest of ricin, the toxin of Ricinus communis L. seeds
- Author
-
Lucienne J.G. Haas-Kohn, Guy Dirheimer, Orio Ciferri, Alain-AndréJ. Lugnier, and Orsola Tiboni
- Subjects
endocrine system ,Biophysics ,Ricin ,Biology ,medicine.disease_cause ,Biochemistry ,Ribosome ,Hydrolysate ,chemistry.chemical_compound ,Structure-Activity Relationship ,Bacterial Proteins ,medicine ,Protein biosynthesis ,Escherichia coli ,Molecular Biology ,Toxin ,Ricinus ,Cell Biology ,biology.organism_classification ,Peptide Fragments ,carbohydrates (lipids) ,Elongation factor ,enzymes and coenzymes (carbohydrates) ,chemistry ,Protein Biosynthesis ,Ribosomes - Abstract
Protein synthesizing systems derived from crude extracts as well as from partially purified 70S ribosomes and elongation factors from Escherichia coli were treated with ricin, ricin A and B chains or ricin tryptic hydrolysate. Ricin and its isolated chains do not inhibit protein synthesis in these systems. However, a tryptic hydrolysate of ricin inhibits both Escherichia coli protein synthesizing systems. These results demonstrate that, although ricin and its two polypeptides A and B have no activity on Escherichia coli protein synthesis, some tryptic product(s) of ricin are able to inhibit protein synthesis in procaryotes. Thus it appears that fragments smaller than ricin or its two polypeptides can inactivate 70S ribosomes.
- Published
- 1980