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. 1992 Aug 15;286(Pt 1):1–4. doi: 10.1042/bj2860001

Some ribosome-inactivating proteins depurinate ribosomal RNA at multiple sites.

L Barbieri 1, J M Ferreras 1, A Barraco 1, P Ricci 1, F Stirpe 1
PMCID: PMC1133008  PMID: 1520257

Abstract

Saporin-S6, a ribosome-inactivating protein (RIP) from Saponaria officinalis released more than 1 mol of adenine/mol of ribosomes from house fly (Musca domestica) larvae and from rat liver. The release of adenine from rat liver ribosomes by several RIPs (plant enzymes with RNA N-glycosidase activity) was examined. Saporins, pokeweed antiviral protein from roots of Phytolacca americana (PAP-R), and trichokirin from Trichosanthes kirilowii seeds depurinated rat liver ribosomes at more than one site. Up to 33 mol of adenine were released from 1 mol of ribosomes. This property is not common to all RIPS.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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