1887

Abstract

SUMMARY

When purified preparations of the isolate of tobacco rattle virus were stored the protein in the virus particles underwent limited proteolysis. Using polyacrylamide gel electrophoresis, a change was observed in the mol. wt. of the virus polypeptide from 28 500 to 23 500, and in some instances a possible intermediate of 26 000 mol. wt. was detected. Polypeptides of mol. wt. 13 500, 11 500 and 9000 were also detected after prolonged storage. Virus protein was not degraded when virus preparations containing sodium azide or antibiotics were stored, but it was degraded in the presence of azide when incubated with the supernatant fluid obtained by centrifuging preparations of virus which had been stored for several months without bacteriostatic additive. The proteolysis was probably caused by microbial exoenzyme(s). The conversion of polypeptide from mol. wt. 28 500 to 23 500 did not affect sedimentation coefficient, behaviour when centrifuged to equilibrium in caesium chloride, appearance in the electron microscope, serological reactivity, infectivity, heat stability or resistance of infectivity to pancreatic ribonuclease.

Purified virus was not affected by treatment with trypsin or chymotrypsin whereas the virus polypeptide was degraded by pronase and by papain. Papain had effects similar but not identical to those of storage. These enzyme treatments did not greatly affect infectivity or alter the appearance of virus particles in the electron microscope.

Isolate was affected by storage and by papain treatment in the same way as isolate , but more slowly.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-18-3-281
1973-03-01
2021-10-18
Loading full text...

Full text loading...

/deliver/fulltext/jgv/18/3/JV0180030281.html?itemId=/content/journal/jgv/10.1099/0022-1317-18-3-281&mimeType=html&fmt=ahah

References

  1. Barnett O. W., Murant A. F. 1970; Host range, properties and purification of raspberry bushy dwarf virus. Annals of Applied Biology 65:435–449
    [Google Scholar]
  2. Cadman C. H., Harrison B. D. 1959; Studies on the properties of soil-borne viruses of the tobacco rattle type occurring in Scotland. Annals of Applied Biology 47:542–556
    [Google Scholar]
  3. Carpenter J. M., Cook J. M., Gibbs A. J. 1971; Molecular weights of plant virus proteins. Report Rothamsted Experimental Station 1970 p. 122
    [Google Scholar]
  4. Cooper J. I., Mayo M. A. 1972; Some properties of the particles of three tobravirus isolates. Journal of General Virology 16:285–297
    [Google Scholar]
  5. Dunker A. K., Rueckert R. R. 1969; Observations on molecular weight determinations on polyacrylamide gel. Journal of Biological Chemistry 244:5074–5080
    [Google Scholar]
  6. Harrison B. D., Woods R. D. 1966; Serotypes and particle dimensions of tobacco rattle viruses from Europe and America. Virology 28:610–620
    [Google Scholar]
  7. Koenig R., Stegemann H., Francksen H., Paul H. L. 1970; Protein subunits in the potatovirus X group. Determination of the molecular weights by polyacrylamide electrophoresis. Biochimica et biophysica acta 207:184–189
    [Google Scholar]
  8. Lesnaw J. A., Reichmann M. E. 1970; Determination of molecular weights of plant viral protein subunits by polyacrylamide gel electrophoresis. Virology 42:724–731
    [Google Scholar]
  9. Miki T., Okada Y. 1970; Comparative studies on some strains of tobacco rattle virus. Virology 42:993–998
    [Google Scholar]
  10. Niblett C. L., Semancik J. S. 1969; Conversion of the electrophoretic forms of cowpea mosaic virus in vivo and in vitro. Virology 38:685–693
    [Google Scholar]
  11. Offord R. E., Harris J. I. 1965; The protein sub-unit of tobacco rattle virus. Federation of European Biochemical Societies 2nd meeting; abstracts 216 217
    [Google Scholar]
  12. Pereira H. G., Skehel J. J. 1971; Spontaneous and tryptic degradation of virus particles and structural components of adenoviruses. Journal of General Virology 12:13–24
    [Google Scholar]
  13. Rees M. W., Short M. N. 1965; Variations in the composition of two strains of tobacco mosaic virus in relation to their host. Virology 26:596–602
    [Google Scholar]
  14. Semancik J. S. 1970; Identity of structural protein from two isolates of TRV with different length of associated short particles. Virology 40:618–623
    [Google Scholar]
  15. Swank R. T., Munkres K. D. 1971; Molecular weight analysis of oligopeptides by electrophoresis in polyacrylamide gel with sodium dodecyl sulphate. Analytical Biochemistry 39:462–477
    [Google Scholar]
  16. Szbalski W., Szybalski E. H. 1971; Equilibrium density gradient centrifugation. In Procedures in Nucleic Acid Research 2311–354 Edited by Cantoni G. L., Davies D. R. New York and London: Harper & Row;
    [Google Scholar]
  17. Tung J., Knight C. A. 1971; Effect of charge on the determination of molecular weight of proteins by gel electrophoresis in SDS. Biochemical and Biophysical Research Communications 42:1117–1121
    [Google Scholar]
  18. Weber K., Osborn M. 1969; The reliability of molecular weight determination by SDS-polyacrylamide gel electrophoresis. Journal of Biological Chemistry 244:4406–4412
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-18-3-281
Loading
/content/journal/jgv/10.1099/0022-1317-18-3-281
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