Skip to main content
NCBI home page
Journal of Virology logoLink to Journal of Virology
. 1971 Nov;8(5):716–721. doi: 10.1128/jvi.8.5.716-721.1971

Quantitative Binding of 125I-Concanavalin A to Normal and Transformed Cells

Donna J Arndt-Jovin 1,1, Paul Berg 1
PMCID: PMC376252  PMID: 4332142

Abstract

We have measured the quantitative binding of the radioactively labeled agglutinin 125I-concanavalin A to normal mammalian cells and simian virus 40- and polyoma virus-transformed cells from tissue culture. Parallel measurements of the amount of 125I-concanavalin A necessary to cause agglutination of the cells in suspension were carried out. The transformed and nontransformed cells used for these experiments show large differences in their ability to be agglutinated by 125I-concanavalin A. However, these cell lines have the same number of specific binding sites and similar affinities for the agglutinin whether transformed, trypsinized, or nontransformed. We conclude that the differential capacity of concanavalin A to agglutinate transformed cells relative to normal cells does not result from differences in the number of binding sites between the two types of cells.

Full text

PDF
716

Selected References

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

  1. Aub J. C., Sanford B. H., Cote M. N. Studies on reactivity of tumor and normal cells to a wheat germ agglutinin. Proc Natl Acad Sci U S A. 1965 Aug;54(2):396–399. doi: 10.1073/pnas.54.2.396. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BOYD W. C. The lectins: their present status. Vox Sang. 1963 Jan-Feb;8:1–32. doi: 10.1111/j.1423-0410.1963.tb04146.x. [DOI] [PubMed] [Google Scholar]
  3. Burger M. M. A difference in the architecture of the surface membrane of normal and virally transformed cells. Proc Natl Acad Sci U S A. 1969 Mar;62(3):994–1001. doi: 10.1073/pnas.62.3.994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Burger M. M., Goldberg A. R. Identification of a tumor-specific determinant on neoplastic cell surfaces. Proc Natl Acad Sci U S A. 1967 Feb;57(2):359–366. doi: 10.1073/pnas.57.2.359. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Burger M. M., Noonan K. D. Restoration of normal growth by covering of agglutinin sites on tumour cell surface. Nature. 1970 Nov 7;228(5271):512–515. doi: 10.1038/228512a0. [DOI] [PubMed] [Google Scholar]
  6. Cline M. J., Livingston D. C. Binding of 3 H-concanavalin A by normal and transformed cells. Nat New Biol. 1971 Aug 4;232(31):155–156. doi: 10.1038/newbio232155a0. [DOI] [PubMed] [Google Scholar]
  7. Duksin D., Katchalski E., Sachs L. Specific aggregation of SV40-transformed cells by ornithine, leucine copolymers. Proc Natl Acad Sci U S A. 1970 Sep;67(1):185–192. doi: 10.1073/pnas.67.1.185. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. FORRESTER J. A., AMBROSE E. J., MACPHERSON J. A. Electrophoretic investigations of a clone of hamster fibroblasts and polyoma-transformed cells from the same population. Nature. 1962 Dec 15;196:1068–1070. doi: 10.1038/1961068a0. [DOI] [PubMed] [Google Scholar]
  9. Hause L. L., Pattillo R. A., Sances A., Jr, Mattingly R. F. Cell surface coatings and membrane potentials of malignant and nonmalignant cells. Science. 1970 Aug 7;169(3945):601–603. doi: 10.1126/science.169.3945.601. [DOI] [PubMed] [Google Scholar]
  10. Inbar M., Sachs L. Interaction of the carbohydrate-binding protein concanavalin A with normal and transformed cells. Proc Natl Acad Sci U S A. 1969 Aug;63(4):1418–1425. doi: 10.1073/pnas.63.4.1418. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Inbar M., Sachs L. Structural difference in sites on the surface membrane of normal and transformed cells. Nature. 1969 Aug 16;223(5207):710–712. doi: 10.1038/223710a0. [DOI] [PubMed] [Google Scholar]
  12. Kalb A. J., Levitzki A. Metal-binding sites of concanavalin A and their role in the binding of alpha-methyl d-glucopyranoside. Biochem J. 1968 Oct;109(4):669–672. doi: 10.1042/bj1090669. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. Olson M. O., Liener I. E. The association and dissociation of concanavalin A, the phytohemagglutinin of the jack bean. Biochemistry. 1967 Dec;6(12):3801–3808. doi: 10.1021/bi00864a025. [DOI] [PubMed] [Google Scholar]
  15. Ozanne B., Sambrook J. Binding of radioactively labelled concanavalin A and wheat germ agglutinin to normal and virus-transformed cells. Nat New Biol. 1971 Aug 4;232(31):156–160. doi: 10.1038/newbio232156a0. [DOI] [PubMed] [Google Scholar]
  16. Phillips D. R., Morrison M. The arrangement of proteins in the human erythrocyte membrane. Biochem Biophys Res Commun. 1970 Jul 27;40(2):284–289. doi: 10.1016/0006-291x(70)91007-7. [DOI] [PubMed] [Google Scholar]
  17. Pollack R. E., Burger M. M. Surface-specific characteristics of a contact-inhibited cell line containing the SV40 viral genome. Proc Natl Acad Sci U S A. 1969 Apr;62(4):1074–1076. doi: 10.1073/pnas.62.4.1074. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. STECK T. L., HOELZLWALLACH D. F. THE BINDING OF KIDNEY-BEAN PHYTOHEMAGGLUTININ BY EHRLICH ASCITES CARCINOMA. Biochim Biophys Acta. 1965 Mar 8;97:510–522. [PubMed] [Google Scholar]
  19. So L. L., Goldstein I. J. Protein-carbohydrate interaction. XX. On the number of combining sites on concanavalin A, the phytohemagglutinin of the jack bean. Biochim Biophys Acta. 1968 Oct 15;165(3):398–404. doi: 10.1016/0304-4165(68)90218-3. [DOI] [PubMed] [Google Scholar]
  20. Sumner J. B., Howell S. F. Identification of Hemagglutinin of Jack Bean with Concanavalin A. J Bacteriol. 1936 Aug;32(2):227–237. doi: 10.1128/jb.32.2.227-237.1936. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Wang J. L., Cunningham B. A., Edelman G. M. Unusual fragments in the subunit structure of concanavalin A. Proc Natl Acad Sci U S A. 1971 Jun;68(6):1130–1134. doi: 10.1073/pnas.68.6.1130. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES