Purification and partial characterization of single-chain ribosome-inactivating proteins from the seeds of Phytolacca dioica L.

@article{Parente1993PurificationAP,
  title={Purification and partial characterization of single-chain ribosome-inactivating proteins from the seeds of Phytolacca dioica L.},
  author={Augusto Parente and Pasquale De Luca and Andrea Bolognesi and Luigi Barbieri and Maria Giulia Battelli and A. Abbondanza and M. A. J. van de Sande and Gesualdo Siniscalco Gigliano and Pier Luigi Tazzari and Fiorenzo Stirpe},
  journal={Biochimica et biophysica acta},
  year={1993},
  volume={1216 1},
  pages={43-9}
}
Three ribosome-inactivating proteins (RIPs) similar to those already known (Stirpe et al. (1992) Bio/Technology 10, 405-412) were purified from the seeds of Phytolacca dioica. These proteins, called Phytolacca dioica RIPs (PD-S1, PD-S2 and PD-S3 RIPs), are glycoproteins, with M(r) approx. 30,000, inhibit protein synthesis by a rabbit reticulocyte lysate and phenylalanine polymerization by isolated ribosomes, and depurinate rat liver rRNA in an apparently identical manner as the A-chain of ricin… CONTINUE READING