Wheat ribosome-inactivating proteins: Seed and leaf forms with different specificities and cofactor requirements

@article{Massiah1995WheatRP,
  title={Wheat ribosome-inactivating proteins: Seed and leaf forms with different specificities and cofactor requirements},
  author={Andrea J. Massiah and Martin R. Hartley},
  journal={Planta},
  year={1995},
  volume={197},
  pages={633-640}
}
Distinct forms of ribosome-inactivating proteins were purified from wheat (Triticum aestivum L.) germ and leaves and termed tritin-S and tritin-L, respectively. These differ in size and charge and are antigenically unrelated. They are both RNA N-glycosidases which act on 26S rRNA in native yeast (Saccharomyces cerevisiae) ribosomes by the removal of A3024 located in a universally conserved sequence in domain VII which has previously been identified as the site of action of ricin A-chain. Tritin… CONTINUE READING

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