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      Dependence of depurination of oligoribonucleotides by ricin A-chain on divalent cations and chelating agents.

      1 ,
      Biochemistry and molecular biology international
      Informa UK Limited

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          Abstract

          Ricin A-chain is a cytotoxic RNA N-glycosidase that inactivates eukaryotic ribosomes by depurinating the adenosine at position 4324 in 28S rRNA. The enzyme retains its specificity when a synthetic oligoribonucleotide (a 35-mer) that mimics the structure at the site of action is the substrate. However, covalent modification by ricin A-chain of the oligoribonucleotide but not of ribosomes, depends on the simultaneous presence of a divalent cation and a chelating agent.

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          Author and article information

          Journal
          Biochem. Mol. Biol. Int.
          Biochemistry and molecular biology international
          Informa UK Limited
          1039-9712
          1039-9712
          May 1996
          : 39
          : 2
          Affiliations
          [1 ] Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637, USA.
          Article
          10.1080/15216549600201301
          8799455
          aaf2211e-2636-403a-a19a-06b16d826d0f
          History

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