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. 1977 Mar;74(3):818–821. doi: 10.1073/pnas.74.3.818

Eukaryote ribosomes possess a binding site for concanavalin A.

G A Howard, H P Schnebli
PMCID: PMC430488  PMID: 322153

Abstract

Ribosomes prepared from chicken liver or rabbit reticulocytes bound concanavalin A in a molar ratio of approximately 1:1. This binding is to the large subunit of the eukaryote ribosomes with a dissociation constant of 5 X 10(-7) M (0 degrees). The binding of concanavalin A to Escherichia coli ribosomes was much less. Binding to the RNA or to possible membrane contaminants was ruled out in control experiments. Chicken liver ribosomes were labeled in vivo with 3H-labeled amino acids, purified, and dissociated in sodium dodecyl sulfate. Affinity chromatography of this preparation made it possible to isolate the small proportion of the ribosomal proteins (about 1.5%) containing the concanavalin A binding site. This protein moved as a single band during electrophoresis on polyacrylamide gels containing sodium dodecyl sulfate and showed an apparent molecular weight of 31,000.

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Selected References

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

  1. Dierks-Ventling C., Jost J. P. Effect of 17 beta-estradiol on the synthesis of non-histone nuclear proteins in chick liver. Eur J Biochem. 1974 Dec 16;50(1):33–40. doi: 10.1111/j.1432-1033.1974.tb03870.x. [DOI] [PubMed] [Google Scholar]
  2. Falvey A. K., Staehelin T. Structure and function of mammalian ribosomes. I. Isolation and characterization of active liver ribosomal subunits. J Mol Biol. 1970 Oct 14;53(1):1–19. doi: 10.1016/0022-2836(70)90042-2. [DOI] [PubMed] [Google Scholar]
  3. Feigenson M. E., Schnebli H. P., Baggiolini M. Demonstration of ricin-binding sites on the outer face of azurophil and specific granules of rabbit polymorphonuclear leukocytes. J Cell Biol. 1975 Jul;66(1):183–188. doi: 10.1083/jcb.66.1.183. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Glew R. H., Kayman S. C., Kuhlenschmidt M. S. Studies on the binding of concanavalin A to rat liver mitochondria. J Biol Chem. 1973 May 10;248(9):3137–3145. [PubMed] [Google Scholar]
  5. Henning R., Uhlenbruck G. Detection of carbohydrate structures on isolated subcellular organelles of rat liver by heterophile agglutinins. Nat New Biol. 1973 Mar 28;242(117):120–122. doi: 10.1038/newbio242120a0. [DOI] [PubMed] [Google Scholar]
  6. Howard G. A., Traugh J. A., Croser E. A., Traut R. R. Ribosomal proteins from rabbit reticulocytes: number and molecular weights of proteins from ribosomal subunits. J Mol Biol. 1975 Apr 15;93(3):391–404. doi: 10.1016/0022-2836(75)90285-5. [DOI] [PubMed] [Google Scholar]
  7. Huet C., Lonchampt M., Huet M., Bernadac A. Temperature effects on the concanavalin A molecule and on concanavalin A binding. Biochim Biophys Acta. 1974 Sep 13;365(1):28–39. doi: 10.1016/0005-2795(74)90247-5. [DOI] [PubMed] [Google Scholar]
  8. Jost J. P., Keller R., Dierks-Ventling C. Deoxyribonucleic acid and ribonucleic acid synthesis during phosvitin induction by 17beta-estradiol in immature chicks. J Biol Chem. 1973 Aug 10;248(15):5262–5266. [PubMed] [Google Scholar]
  9. Keenan T. W., Franke W. W., Kartenbeck J. Concanavalin A binding by isolated plasma membranes and endomembranes from liver and mammary gland. FEBS Lett. 1974 Aug 30;44(3):274–278. doi: 10.1016/0014-5793(74)81156-7. [DOI] [PubMed] [Google Scholar]
  10. Lin J. Y., Liu K., Chen C. C., Tung T. C. Effect of crystalline ricin on the biosynthesis of protein, RNA, and DNA in experimental tumor cells. Cancer Res. 1971 Jul;31(7):921–924. [PubMed] [Google Scholar]
  11. Monneron A., Segretain D. Extensive binding of concanavalin A to the nuclear membrane. FEBS Lett. 1974 Jun 1;42(2):209–213. doi: 10.1016/0014-5793(74)80787-8. [DOI] [PubMed] [Google Scholar]
  12. Nicolson G. L. The interactions of lectins with animal cell surfaces. Int Rev Cytol. 1974;39:89–190. doi: 10.1016/s0074-7696(08)60939-0. [DOI] [PubMed] [Google Scholar]
  13. Nicolson G., Lacorbière M., Delmonte P. Outer membrane terminal saccharides of bovine liver nuclei and mitochondria. Exp Cell Res. 1972;71(2):468–473. doi: 10.1016/0014-4827(72)90318-7. [DOI] [PubMed] [Google Scholar]
  14. Smith R. L., Baca O., Gordon J. Co-ordinate synthesis of ribosomes and elongation factors in the liver of immature chicks following a metabolic shift up. J Mol Biol. 1976 Jan 15;100(2):115–126. doi: 10.1016/s0022-2836(76)80143-x. [DOI] [PubMed] [Google Scholar]
  15. Smith R. L., Gordon J. Preparation of avian ribosomes with low levels of contaminating elongation factors. FEBS Lett. 1974 Jul 15;43(2):223–226. doi: 10.1016/0014-5793(74)81005-7. [DOI] [PubMed] [Google Scholar]
  16. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]

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