1887

Abstract

SUMMARY

Proteolytic digestion of the M-protein of Sendai virus produces a product with a mol. wt. approximately 5000 less than that of the intact protein. In the case of digestion with chymotrypsin this cleavage is quite specific and the cleaved protein can be isolated. The smaller fragment appears to be physically removed from the larger (30000 mol. wt.) fragment, rather than remaining in non-covalent association with it. The cleavage is likely to be near the N-terminus of the protein. At the present time there is no indication of the biological function of this fragment.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-39-2-311
1978-05-01
2022-01-25
Loading full text...

Full text loading...

/deliver/fulltext/jgv/39/2/JV0390020311.html?itemId=/content/journal/jgv/10.1099/0022-1317-39-2-311&mimeType=html&fmt=ahah

References

  1. Brand C. M., Skehel J. J. 1972; Crystalline antigen from the influenza virus envelope. Nature New Biology 238:145–147
    [Google Scholar]
  2. Bruton C. J., Hartley B. S. 1970; Chemical studies of methionyl-tRNA synthetase from E. coli. Journal of Molecular Biology 53:165–178
    [Google Scholar]
  3. Edelhoch H. 1967; Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6:1948–1954
    [Google Scholar]
  4. Gray W. R. 1972; End group analysis using dansyl chloride. In Methods in Enzymology vol XXV pp 121–138 Edited by Hirs C. H. W., Timasheff S. N. New York: Academic Press;
    [Google Scholar]
  5. Guidotti G. 1960; The action, of carboxypeptidases A and B on the separated α and β chains of normal adult human hemoglobin. Biochimica et Biophysica Acta 42:177–179
    [Google Scholar]
  6. Hewitt J. A. 1977; Studies on the subunit composition of the M-protein of Sendai virus. FEBS Letters 81:395–398
    [Google Scholar]
  7. Hewitt J. A., Nermut M. V. 1977; A morphological study of the M-protein of Sendai virus. Journal of General Virology 34:127–136
    [Google Scholar]
  8. Hirs C. H. W. 1967; Performic acid oxidation. In Methods in Enzymology vol XI pp 197–199 Edited by Hirs C. H. W. New York: Academic Press;
    [Google Scholar]
  9. Moore S. 1972; The precision and sensitivity of amino acid analysis. In Chemistry and Biology of Peptides pp 629–653 Edited by Meinhoffer J. Ann Arbor: Ann Arbor Science Publishers Inc;
    [Google Scholar]
  10. Segrest J. P., Jackson R. L., Marchesi V. T., Guyer R. B., Terry W. 1972; Red cell membrane glycoprotein: amino acid sequence of an intramembranous region. Biochemical & Biophysical Research Communication 49:964–969
    [Google Scholar]
  11. Spatz L., Strittmatter P. 1971; A form of cytochrome b5 that contains an additional hydrophobic sequence of 40 amino acid residues. Proceedings of the National Academy of Sciences of the United States of America 68:1042–1046
    [Google Scholar]
  12. Utermann G., Simons K. 1974; Studies on the amphipathic nature of the membrane proteins in Semliki Forest virus. Journal of Molecular Biology 85:569–588
    [Google Scholar]
  13. Weiner A. M., Platt T., Weber K. 1972; Amino-terminal sequence analysis of proteins purified on a nanomole scale by gel electrophoresis. Journal of Biological Chemistry 247:3242–3251
    [Google Scholar]
  14. Yamada S., Hans H. A. 1966; Phenanthrequinone as an analytical reagent for arginine. Biochimica et Biophysica Acta 130:538–540
    [Google Scholar]
  15. Yoshida T., Nagai Y., Yoshii S., Maeno K., Matsumoto T., Hoshino M. 1976; Membrane (M) protein of HVJ (Sendai virus): its role in virus assembly. Virology 71:143–161
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-39-2-311
Loading
/content/journal/jgv/10.1099/0022-1317-39-2-311
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

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