1887

Abstract

SUMMARY

The encephalomyocarditis (EMC) virus particle appears to contain about 60 chains each of four major polypeptides and 2 chains of a minor component. Two major polypeptides were assumed to have the same mol. wt. of 32000 since they were not separated by electrophoresis on polyacrylamide gels containing SDS, although they are separable by calcium phosphate chromatography. The two other major polypeptides appeared to be homogeneous when examined by calcium phosphate chromatography; they have mol. wt. of 25000 and 11000, based upon gel electrophoresis, although examination of the latter polypeptide by gel filtration in the presence of 6 -guanidine gave a mol. wt. of 6700. The minor component has a mol. wt., determined by gel electrophoresis, of about 42000.

Similar results were obtained for the closely related Mouse-Elberfeld (ME) virus except that two polypeptides of mol. wt. 33000 and 30800, were found rather than two of 32000. Since the ME and EMC viruses studied were both grown in Krebs II ascites tumour cells, the differences in mol. wt. of the polypeptides probably reflected differences either in the specificity of the cleavage enzyme or in the amino acid sequence in the cleavage region.

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1974-06-01
2022-09-25
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References

  1. Bellett A. J. D., Burness A. T. H. 1963; Intracellular sites of synthesis of encephalomyocarditis virus components in Krebs-2 ascites tumour cells. Journal of General Microbiology 30:131–140
    [Google Scholar]
  2. Buchanan J. M., Hartman S. C. 1959; Enzymic reactions in the synthesis of the purines. In Advances in Enzymology 21199–261 Edited by Nord F. F. New York: Interscience Publishers, Inc;
    [Google Scholar]
  3. Burness A. T. H. 1967; Separation of plaque-type variants of encephalomyocarditis virus by chromatography on calcium phosphate. Journal of Virology 1:308–316
    [Google Scholar]
  4. Burness A. T. H. 1969a; Purification of encephalomyocarditis virus. Journal of General Virology 5:291–303
    [Google Scholar]
  5. Burness A. T. H. 1969b; Purification and separation of encephalomyocarditis virus variants by chromatography on calcium phosphate. In Fundamental Techniques in Virology Edited by Habel K., Salzman N. New York and London: Academic Press;
    [Google Scholar]
  6. Burness A. T. H. 1970; Ribonucleic acid content of encephalomyocarditis virus. Journal of General Virology 6:373–380
    [Google Scholar]
  7. Burness A. T. H., Clothier F. W. 1970; Particle weight and other biophysical properties of encephalomyocarditis virus. Journal of General Virology 6:381–393
    [Google Scholar]
  8. Burness A. T. H., Pardoe I. U. 1971; Further studies on a purification procedure for encephalomyocarditis virus. Journal of General Virology 12:187–190
    [Google Scholar]
  9. Burness A. T. H., Pardoe I. U., Fox S. M. 1972; Separation of encephalomyocarditis virus capsid polypeptides on calcium phosphate. Communication 3559 Federation Proceedings 31:
    [Google Scholar]
  10. Burness A. T. H., Pardoe I. U., Fox, S. M. 1973; Evidence for the lack of glycoprotein in the encephalomyocarditis virus particle. Journal of General Virology 18:33–49
    [Google Scholar]
  11. Burness A. T. H., Walter D. S. 1967; Protein components of encephalomyocarditis virus. Nature, London 215:1350–1352
    [Google Scholar]
  12. Butterworth B. E., Hall L., Stolzfus C. M., Rueckert R. R. 1971; Virus-specific proteins synthesised in encephalomyocarditis virus infected HeLa cells. Proceedings of the National Academy of Sciences of the United States of America 68:3083–3087
    [Google Scholar]
  13. Caspar D. L. D., Klug A. 1962; Physical principles in the construction of regular viruses. Cold Spring Harbor Symposium 27:1–24
    [Google Scholar]
  14. Chrambach A., Reisfeld R. A., Wykoff M., Zaccari J. 1967; A procedure for rapid and sensitive staining of protein fractionated by polyacrylamide gel electrophoresis. Analytical Biochemistry 20:150–154
    [Google Scholar]
  15. Crick F. H. C., Watson J. D. 1956; Structure of small viruses. Nature, London 17:473–475
    [Google Scholar]
  16. Crick F. H. C., Watson J. D. 1957; Virus structure: general principles. In Ciba Foundation Symposium on The Nature of Viruses pp 5–13 Edited by Wolstenholme E. W., Millar E. C. P. London: Churchill;
    [Google Scholar]
  17. Dobos P., Martin E. M. 1972; Virus-specific polypeptides in ascites cells infected with encephalomyocarditis virus. Journal of General Virology 17:197–212
    [Google Scholar]
  18. Dunker A. K., Rueckert R. R. 1969; Observations on molecular weight determinations on polyacrylamide gel. Journal of Biological Chemistry 244:5074–5080
    [Google Scholar]
  19. Dunker A. K., Rueckert R. R. 1971; Fragments generated by pH dissociation of ME-virus and their relation to the structure of the virion. Journal of Molecular Biology 58:217–235
    [Google Scholar]
  20. Fenner F. 1968; The biology of animal viruses. In Molecular and Cellular Biology vol 1 New York and London: Academic Press;
    [Google Scholar]
  21. Fish W. W., Mann K. G., Tanford C. 1969; The estimation of polypeptide chain molecular weights by gel filtration in 6 M guanidine hydrochloride. Journal of Biological Chemistry 244:4989–4994
    [Google Scholar]
  22. Fiske C. H., Subbarow Y. 1925; The colorimetric determination of phosphorus. Journal of Biological Chemistry 66:375–400
    [Google Scholar]
  23. Hall L. 1970; Infection of tissue culture cells by cardioviruses. Ph.D. Thesis University of Wisconsin;
    [Google Scholar]
  24. Hoskins J. M., Sanders F. K. 1957; Propagation of mouse encephalomyocarditis virus in ascites tumour cells maintained in vitro. British Journal of Experimental Pathology 38:268–272
    [Google Scholar]
  25. Jacobson M. F., Baltimore D. 1968; Polypeptide cleavages in the formation of poliovirus proteins. Proceedings of the National Academy of Sciences of the United States of America 61:77–84
    [Google Scholar]
  26. O’Callaghan D. J., Mak T. W., Colter J. S. 1970; Studies of the protein subunit of pH-inactivated Mengo virus variants. 1. Polypeptide composition. Virology 42:229–233
    [Google Scholar]
  27. Rueckert R. R. 1965; Studies on the structure of viruses of the Columbia SK group.II. The protein subunits of ME-Virus and other members of the Columbia SK group. Virology 26:345–358
    [Google Scholar]
  28. Rueckert R. R. 1971; Picornaviral architecture. In Comparative Virology255–306 Edited by Maramorosch K., Kurstak E. New York and London: Academic Press;
    [Google Scholar]
  29. Rueckert R. R., Dunker A. K., Stolzfus C. M. 1969; The structure of Mouse-Elberfeld virus: a model. Proceedings of the National Academy of Sciences of the United States of America 62:912–919
    [Google Scholar]
  30. Sanders F. K., Huppert J., Hoskins J. M. 1958; Replication of an animal virus. Symposia of the Society for Experimental Biology 12:123–137
    [Google Scholar]
  31. Shapiro A. L., Vinuela E., Maizel J. V. 1967; Molecular weight estimation of polypeptide chains by electrophoresis in SDS polyacrylamide gels. Biochemical and Biophysical Research Communications 28:815–820
    [Google Scholar]
  32. Stolzfus C. M., Rueckert R. 1972; Capsid polypeptides of Mouse-Elberfeld virus. 1. Amino acid compositions and molar ratios in the virion. Journal of Virology 10:347–355
    [Google Scholar]
  33. Summers D. F., Maizel J. V. 1968; Evidence for large precursor proteins in poliovirus synthesis. Proceedings of the National Academy of Sciences of the United States of America 59:966–971
    [Google Scholar]
  34. Weber K., Osborn M. 1969; The reliability of molecular weight determinations by dodecyl sulfate polyacrylamide gel electrophoresis. Journal of Biological Chemistry 244:4406–4412
    [Google Scholar]
  35. Work T. S. 1964; Electrophoretic separation of the proteins of ribosome subunits and of encephalomyocarditis virus. Journal of Molecular Biology 10:544–545
    [Google Scholar]
  36. Young R. W., Fulhorst H. W. 1965; Recovery of S35 radioactivity from protein-bearing polyacrylamide gel. Analytical Biochemistry 11:389–391
    [Google Scholar]
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