1887

Abstract

Summary

Chick interferon (IFN), produced in primary chick embryo (CE) cells stimulated by u.v.-irradiated Newcastle disease virus, was partially purified by two-step chromatography using both controlled pore glass and Blue Sepharose. The specific activity of the IFN increased about 500-fold by this method and the final recovery from starting material was more than 95%. The partially purified IFN was analysed by SDS-PAGE, and two peaks of IFN activity were observed. The molecular weight represented by the sharp peak was estimated to be 18000 (18K) and a broad peak was found at 20K to 30K. Glycosidase treatment before SDS-PAGE resulted in disappearance of the broad peak and increased the activity of the 18K peak. Anti-CE IFN rabbit serum and a monoclonal antibody against the CE IFN neutralized the antiviral activity of all IFN samples prepared under various conditions.

Keyword(s): chicken , IFN and purification
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/content/journal/jgv/10.1099/0022-1317-67-1-215
1986-01-01
2024-04-23
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References

  1. Finter N. B. 1969; Dye uptake methods for assessing viral cytopathogenicity and their application to interferon assays. Journal of General Virology 5:419–427
    [Google Scholar]
  2. Fujisawa J., Kawade Y. 1981; Properties of nonglycosylated and glycosidase-treated mouse L cell interferon species. Virology 112:480–487
    [Google Scholar]
  3. Fujita T., Kohno S. 1981; Studies on interferon priming: cellular response to viral and nonviral inducers and requirement for protein synthesis. Viology 112:62–69
    [Google Scholar]
  4. Havell E. A., Berman B., Ogburn C. A., Berg K., Paucker K., Vilček J. 1975; Two antigenically distinct species of human interferon. Proceedings of the National Academy of Sciences, U.S.A 72:2185–2187
    [Google Scholar]
  5. Havell E. A., Yamazaki S., Vilček J. 1977; Altered molecular species of human interferon produced in the presence of inhibitors of glycosylation. Journal of Biological Chemistry 252:4425–4427
    [Google Scholar]
  6. Isaacs A., Lindenmann J. 1957; Virus interference. I. The interferon. Proceedings of the Royal Society B147:258–267
    [Google Scholar]
  7. Kohase M., Kohno S. 1983; Temperature-sensitive mutants of Newcastle disease virus affecting interferon induction. Journal of General Virology 64:1469–1474
    [Google Scholar]
  8. Oie H., Buckler C. E., Uhlendorf C. P., Hill D. H. 1972; Improved assay for a variety of interferon. Proceedings of the Society for Experimental Biology and Medicine 140:1178–1181
    [Google Scholar]
  9. Otto M. J., Sedmak J. J., Grossberg S. E. 1980; Enzymatic modification of human fibroblast and leukocyte interferons. Journal of Virology 35:390–399
    [Google Scholar]
  10. Sato T. A., Fukuda A., Sugiura A. 1985; Characterization of major structural proteins of measles virus with monoclonal antibodies. Journal of General Virology 66:1397–1409
    [Google Scholar]
  11. Stewart W. E. II, Chudzio T., Lin L. S., Wiranowska-Stewart M. 1978; Interferoids: in vitro and in vivo production of modified interferons. Proceedings of the National Academy of Sciences, U.S.A 75:4814–4818
    [Google Scholar]
  12. Yamamoto Y., Kawade Y. 1980; Antigenicity of mouse interferons: distinct antigenicity of the two L cell interferon species. Virology 103:80–88
    [Google Scholar]
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