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  • Title: Alpha-sarcin impairs the N-glycosidase activity of ricin on ribosomes.
    Author: Sperti S, Zamboni M, Brigotti M, Rambelli F, Montanaro L.
    Journal: Biochem Biophys Res Commun; 1989 Apr 28; 160(2):857-61. PubMed ID: 2719703.
    Abstract:
    In a recently described method the RNA N-glycosidase activity of ricin is measured by h.p.l.c. determination of the adenine released from ribosomes after conversion of the base into its fluorescent 1-N6-etheno derivative [Zamboni et al. (1989) Biochem. J., 259, in press]. Unlike previously available methods, based on the separation of RNA fragments by gel electrophoresis, the new method allows one to investigate the activity of ricin on ribosomes pretreated with alpha-sarcin, a cytotoxin which cleaves 28S rRNA at one nucleotide distance from the site of attack of ricin. alpha-Sarcin makes ribosomes a poor substrate for ricin, the release of adenine requiring concentrations of ricin 50-times higher than those effective on untreated ribosomes.
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