Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1980 Jun 15;188(3):941–944. doi: 10.1042/bj1880941

Differential effects of nitrated ricin and nitrated and dithionite-reduced ricin on protein-synthesis inhibition and transmembrane tramsport in eukaryotic cells.

P N Dalrymple, L L Houston
PMCID: PMC1161983  PMID: 7470048

Abstract

Ricin, was nitrated with tetranitromethane and reduced with sodium dithionite. Of the 8.0 nitro groups incorporated, 3.2 were on the A chain and 5.1 were on the B chain. Nitrated ricin1 was somewhat less active than nitrated and reduced ricin1 in inhibiting protein synthesis in vitro, but both were highly inhibitory. However, the modified toxins were less than 1% as active as ricin in inhibiting protein synthesis in cultured cells. Indirect immunofluorescence assays demonstrated tha both modified toxins were specifically bound to the cell surface and could be displaced by galactose.

Full text

PDF
941

Images in this article

943Fig. 2.
on p.943

Selected References

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

  1. Cawley D. B., Hedblom M. L., Hoffman E. J., Houston L. L. Differential ricin sensitivity of rat liver and wheat germ ribosomes in polyuridylic acid translation. Arch Biochem Biophys. 1977 Aug;182(2):690–695. doi: 10.1016/0003-9861(77)90550-1. [DOI] [PubMed] [Google Scholar]
  2. Cawley D. B., Hedblom M. L., Houston L. L. Homology between ricin and Ricinus communis agglutinin: amino terminal sequence analysis and protein synthesis inhibition studies. Arch Biochem Biophys. 1978 Oct;190(2):744–755. doi: 10.1016/0003-9861(78)90335-1. [DOI] [PubMed] [Google Scholar]
  3. Gottlieb C., Kornfeld S. Isolation and characterization of two mouse L cell lines resistant to the toxic lectin ricin. J Biol Chem. 1976 Dec 25;251(24):7761–7768. [PubMed] [Google Scholar]
  4. Hedblom M. L., Cawley D. B., Boguslawski S., Houston L. L. Binding of ricin A chain to rat liver ribosomes: relationship to ribosome inactivation. J Supramol Struct. 1978;9(2):253–268. doi: 10.1002/jss.400090210. [DOI] [PubMed] [Google Scholar]
  5. Hedblom M. L., Cawley D. B., Houston L. L. The specific binding of ricin and its polypeptide chains to rat liver ribosomes and ribosomal subunits. Arch Biochem Biophys. 1976 Nov;177(1):46–55. doi: 10.1016/0003-9861(76)90414-8. [DOI] [PubMed] [Google Scholar]
  6. KITOS P. A., SINCLAIR R., WAYMOUTH C. Glutamine metabolism by animal cells growing in a synthetic medium. Exp Cell Res. 1962 Aug;27:307–316. doi: 10.1016/0014-4827(62)90233-1. [DOI] [PubMed] [Google Scholar]
  7. Meager A., Ungkitchanukit A., Hughes R. C. Variants of hamster fibroblasts resistant to Ricinus communis toxin (ricin). Biochem J. 1976 Jan 15;154(1):113–124. doi: 10.1042/bj1540113. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Nicolson G. L., Lacorbiere M., Hunter T. R. Mechanism of cell entry and toxicity of an affinity- purified lectin from Ricinus communis and its differential effects on normal and virus-transformed fibroblasts. Cancer Res. 1975 Jan;35(1):144–155. [PubMed] [Google Scholar]
  9. Olsnes S., Pihl A. Different biological properties of the two constituent peptide chains of ricin, a toxic protein inhibiting protein synthesis. Biochemistry. 1973 Jul 31;12(16):3121–3126. doi: 10.1021/bi00740a028. [DOI] [PubMed] [Google Scholar]
  10. Riordan J. F., Sokolovsky M., Vallee B. L. Environmentally sensitive tyrosyl residues. Nitration with tetranitromethane. Biochemistry. 1967 Jan;6(1):358–361. doi: 10.1021/bi00853a053. [DOI] [PubMed] [Google Scholar]
  11. Sandvig K., Olsnes S., Pihl A. Binding, uptake and degradation of the toxic proteins abrin and ricin by toxin-resistant cell variants. Eur J Biochem. 1978 Jan 2;82(1):13–23. doi: 10.1111/j.1432-1033.1978.tb11992.x. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES