| Literature DB >> 3360143 |
Abstract
The site of action of the A-chain of mistletoe lectin (ML-A) from Viscum album on eukaryotic ribosomes was studied. Treatment of rat liver ribosomes with ML-A, followed by treatment of the isolated rRNA with aniline, caused the release of a fragment with about 450 nucleotides from 28 S rRNA. Further analysis of nucleotide sequences of this fragment revealed that the aniline-sensitive site of phosphodiester bond was between positions A-4324 and G-4325 in 28 S rRNA. These results indicate that ML-A inactivates the ribosomes by cleaving a N-glycosidic bond at A-4324 of 28 S rRNA in the ribosomes as ricin A-chain does.Entities:
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Year: 1988 PMID： 3360143 DOI： 10.1016/0014-5793(88)80853-6
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124