1887

Abstract

SUMMARY

Binding of L cell interferon to lectins, agglutinin (WFA) and concanavalin A (Con A) was studied by affinity chromatography. Of the two molecular species of L cell interferon, F (mol. wt. 24000) and S (mol. wt. 36000), only the latter was bound efficiently to WFA-Sepharose and eluted quantitatively with -galactose followed by a pH 3 buffer, suggesting a substantial difference between the two interferon species in their carbohydrate structure. Both were partially bound to Con A-Sepharose and eluted with α-methyl--glucoside, indicating that at least some of the F species are also glycoprotein, and that both F and S interferons are heterogeneous as regards their affinity to this lectin.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-42-3-533
1979-03-01
2024-12-13
Loading full text...

Full text loading...

/deliver/fulltext/jgv/42/3/JV0420030533.html?itemId=/content/journal/jgv/10.1099/0022-1317-42-3-533&mimeType=html&fmt=ahah

References

  1. Axen R., Porath J., Ernback S. 1967; Chemical coupling of peptides and proteins to polysaccharides by means of cyanogen halides. Nature, London 24:1302–1304
    [Google Scholar]
  2. Besançon F., Bourgeade M. F. 1974; Affinity of murine and human interferon for Concanavalin A. Journal of Immunology 113:1061–1063
    [Google Scholar]
  3. Bose S., Gurari-rotman D., Ruegg U. T., Corley L., Anfinsen C. B. 1976; Apparent dispensability of the carbohydrate moiety of human interferon for antiviral activity. Journal of Biological Chemistry 251:1659–1662
    [Google Scholar]
  4. Davey M. W., Huang I. W., Sulkowski E., Carter W. A. 1974; Hydrophobic interaction of human interferon with Concanavalin A-agarose. Journal of Biological Chemistry 249:6354–6355
    [Google Scholar]
  5. Davey M. W., Sulkowski E., Carter W. A. 1976; Purification and characterization of mouse interferon with novel affinity sorbents. Journal of Virology 17:439–445
    [Google Scholar]
  6. Dorner F., Scriba M., Weil R. 1973; Interferon: evidence for its glycoprotein nature. Proceedings of the National Academy of Sciences of the United States of America 70:1981–1985
    [Google Scholar]
  7. Havell E. A., Vilcek J., Falcoff E., Berman B. 1975; Suppression of human interferon production by inhibitors of glycosylation. Virology 63:475–483
    [Google Scholar]
  8. Irimura T., Kawaguchi T., Terao T., Osawa T. 1975; Carbohydrate-binding specificity of the so-called galactose-specific phytohemagglutinins. Carbohydrate Research 39:317–327
    [Google Scholar]
  9. Iwakura Y., Yonehara S., Kawade Y. 1978; Purification of mouse L cell interferon: essentially pure preparation with associated cell growth inhibitory activity. Journal of Biological Chemistry 253:5074–5079
    [Google Scholar]
  10. Kawade Y., Matsuzawa T., Yamamoto Y., Tsukui K., Iwakura Y. 1976; A rapid and precise microassay of interferon based on the inhibition of viral RNA synthesis. Annual Report of the Institute for Virus Research, Kyoto University 16:52–58
    [Google Scholar]
  11. Kawade Y., Yamamoto Y., Iwakura Y., Tsukui K., Yonehara S. 1978; Mouse interferon: purification and some chemical and biological properties. In Molecular Basis of Host-Virus Interaction (in the press) Edited by Chakrovorty M. Princeton, NJ.: Science Press;
    [Google Scholar]
  12. Marshall R. D., Neuberger A. 1972; Hen’s egg albumin. In Glycoproteins: Their Composition, Structure and Function part B pp 732–757 Edited by Gottschalk A. Amsterdam: Elsevier;
    [Google Scholar]
  13. Matsuzawa T., Kawade Y. 1974; Cell growth inhibitory activity of electrophoretic fractions of L cell interferon preparation. Acta Virologica 18:383–390
    [Google Scholar]
  14. DeMaeyer-guignard J., Tovey M. G., Gresser L., De maeyer E. 1978; Purification of mouse interferon by sequential affinity chromatography on poly(U)- and antibody-agarose columns. Nature, London 271:622–625
    [Google Scholar]
  15. Ohwaki M., Kawade Y. 1972; Inhibition of multiplication of mouse cells in culture by interferon preparations. Acta Virologica 16:477–486
    [Google Scholar]
  16. Schonne E., Billiau A., Desomer P. 1970; The properties of interferon. IV. Isoelectric focusing of rabbit interferon (NDV-RK13). In International Symposium in Standardization of Interferon and Interferon Inducers vol 14 pp 61–68 Edited by Perkins F. T., Regamy R. Basel: Karger;
    [Google Scholar]
  17. Stewart W. E. I, Legoff S., Wiranowska-stewart M. 1977; Characterization of two distinct molecular populations of type 1 mouse interferons. Journal of General Virology 37:277–284
    [Google Scholar]
  18. Svenson S., Hammarstrom S. G., Kabat E. A. 1970; The effect of borate on polysaccharide-protein and antigen-antibody reactions and its use for purification and fractionation of cross-reacting antibodies. Immunochemistry 7:413–422
    [Google Scholar]
  19. Tsuda M., Kurokawa T., Takeuchi M., Sugino Y. 1975; Changes in cell surface structure by viral transformation studied by binding of lectins differing in sugar specificity. Gann 66:513–521
    [Google Scholar]
  20. Yamamoto Y., Kawade Y. 1976; Purification of two components of mouse L cell interferon: electrophoretic demonstration of interferon proteins. Journal of General Virology 33:225–236
    [Google Scholar]
/content/journal/jgv/10.1099/0022-1317-42-3-533
Loading
/content/journal/jgv/10.1099/0022-1317-42-3-533
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error