1887

Abstract

SUMMARY

Treatment of T3 with various denaturing agents produced distinct components which were identified in the ultracentrifuge. Combining this analysis with electron microscopy made it possible to identify the capsid and nucleocapsid, and a fragment having an , w = 105 ± 10S. This fragment appeared spherical in the electron microscope and had dimensions between 12 nm and 16 nm. It was tentatively identified as the tail. The mol. wt. of the 105S particle and the empty head (200S) were calculated to be 2.3 × 10 and 21.7 × 10, respectively. Adding these weights to the estimated weight for DNA (25 × 10, Lang & Coates, 1968) gave a total weight for the phage of 49 × 10, equal to the mol. wt. obtained by Swaby (1959). In addition to these large fragments, two peptides were examined, one had a mol. wt. of 9300 ± 1400 in 6 -GuHCl (1.5S) and appeared to be a single chain; the other, released when a suspension of phage was diluted, had a mol. wt. of less than 10000. The origins of the two peptides remain largely speculative, but in view of the marked associative properties of the 1.5S peptide and its detection only when the head was destroyed, it is likely that it was a binding fraction in the head of the phage. The second peptide may be more intimately associated with the DNA of T3.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-25-2-187
1974-11-01
2022-08-18
Loading full text...

Full text loading...

/deliver/fulltext/jgv/25/2/JV0250020187.html?itemId=/content/journal/jgv/10.1099/0022-1317-25-2-187&mimeType=html&fmt=ahah

References

  1. Anderson N. G., Cline G. B. 1967; Zonal centrifugation in separation of viruses. Methods in Virology 2:137–178
    [Google Scholar]
  2. Anderson T. F. 1950; Destruction of bacterial viruses by osmotic shock. Journal of Applied Physics 21:70
    [Google Scholar]
  3. Anderson T. F., Rappaport C., Mascatine N. A. 1953; On the structure and osmotic properties of phage particles. Annals of the Institute of Pasteur 84:5–15
    [Google Scholar]
  4. Ansevin A. T., Lauffer M. A. 1959; Native tobacco mosaic virus protein of molecular weight 18000. Nature, London 183:1601–1602
    [Google Scholar]
  5. Bancroft J. B., Hills G. J., Markham R. 1967; A study of self-assembly process in a small spherical virus. Virology 31:354–379
    [Google Scholar]
  6. Barnett W. A. 1972; Physico-chemical studies of T3 proteins. Ph.D. Thesis University of Birmingham;
    [Google Scholar]
  7. Barnett W. A., Spragg S. P. 1971; Estimation of molecular weights of protein-SDS complexes. Nature New Biology 234:191–192
    [Google Scholar]
  8. Bendet I. 1962; The size of T3 DNA. Journal of Molecular Biology 5:76–79
    [Google Scholar]
  9. Cassassa E. F., Eisenberg H. A. 1964; Thermodynamic analysis of multicomponent solutions. Advances in Protein Chemistry 19:287–395
    [Google Scholar]
  10. Cohn E. J., Edsall J. T. 1950 In Proteins, Amino Acids and Peptides 375 4th Edit American Chemical Society Monograph Series No. 90;
    [Google Scholar]
  11. Dyson R. D. 1966; A procedure for the extraction of DNA and protein ghosts from bacteriophage lambda. Biochemical and Biophysical Research Communications 22:106–111
    [Google Scholar]
  12. Dyson R. D., van Holde K. E. 1967; An investigation of bacteriophage lambda, its protein ghosts and sub-units. Virology 33:559–566
    [Google Scholar]
  13. Edmunson A. B., Hirs C. H. W. 1962; On the structure of sperm whale myoglobin, 1. The amino acid composition and terminal groups of the chromatographically purified protein. Journal of Molecular Biology 5:663–682
    [Google Scholar]
  14. Fraser D., Jerrel E. 1953; The amino acid composition of T3 bacteriophage. Journal of Biological Chemistry 205:291–302
    [Google Scholar]
  15. Hohn T. 1969; Role of RNA in the assembly process of bacteriophage f5. Journal of Molecular Biology 43:191–200
    [Google Scholar]
  16. Knight C. 1954; The chemical constitution of viruses. Advances in Virus Research 2:153–182
    [Google Scholar]
  17. Lang D., Coates P. 1968; Diffusion coefficient of DNA in solution at ‘zero’ concentration as measured by electron microscopy. Journal of Molecular Biology 36:137–151
    [Google Scholar]
  18. Leberman R. 1968; The disaggregation and assembly of simple viruses. Symposium of Society of General Microbiology 18:183–205
    [Google Scholar]
  19. Lee J. C., Timasheff S. N. 1974; Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride. Biochemistry 13:257–265
    [Google Scholar]
  20. Morrod R. S. 1969; The optimization of density gradients for zonal centrifugation. Ph.D. Thesis University of Birmingham;
    [Google Scholar]
  21. Patterson M. S., Greene R. S. 1965; Measurement of low energy beta-emitters in aqueous solution by liquid scintillation counting of emissions. Analytical Chemistry 37:854–857
    [Google Scholar]
  22. Richards E. G., Teller D. C., Schachman H. K. 1968; Ultracentrifuge studies with Rayleigh interference optics. II. Low-speed sedimentation equilibrium of homogeneous systems. Biochemistry 7:1054–1076
    [Google Scholar]
  23. Schachman H. K. 1959 In Ultracentrifuge in Biochemistry 82 New York: Academic Press;
    [Google Scholar]
  24. Showe M. K., Black L. W. 1973; Assembly core of bacteriophage T4: an intermediate in head formation. Nature New Biology 242:70–71
    [Google Scholar]
  25. Simon L. D., Anderson T. F. 1967; The infection of Escherichia coli by Tz and T4 bacteriophages as seen in the electron microscope. 1. Attachment and penetration. Virology 32:279–297
    [Google Scholar]
  26. Spragg S. P. 1967; Processing ultracentrifuge data with an ‘on-line’ digital computer. Analytica chimica acta 38:137–142
    [Google Scholar]
  27. Spragg S. P., Goodman R. F. 1969; Results from ‘on-line’ processing of ultracentrifuge data with a digital computer. Annals of New York Academy of Sciences 164:294–305
    [Google Scholar]
  28. Spragg S. P., Rankin C. T. 1967; The capacity of zones in density-gradient centrifugation. Biochimica et biophysica acta 141:164–173
    [Google Scholar]
  29. Stibenz D., Mann W., Brandt B., Michel S., Richter G. 1971; Preparation gereinigter T3-phagen und gelelektrophoresische auftrennung ihrer hiillproteine. Acta Biologica et Medica Germanica 27:553–558
    [Google Scholar]
  30. Swaby L. G. 1959; Physical study of T3 bacteriophage. Dissertation Abstracts 20:1567
    [Google Scholar]
  31. Tanford C. 1968; Protein denaturation. Advances in Protein Chemistry 23:121–282
    [Google Scholar]
  32. Tanford C. 1970; Protein denaturation. Part C. Theoretical models for the mechanism of denaturation. Advances in Protein Chemistry 24:1–95
    [Google Scholar]
  33. Theorell H. 1934; Crystalline myoglobin. II. Sedimentation constant and molecular weight of myoglobin. Biochemica Zeitung 268:46–54
    [Google Scholar]
  34. Wilkinson G. N. 1961; Statistical estimations in enzyme kinetics. Biochemical Journal 80:324–332
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-25-2-187
Loading
/content/journal/jgv/10.1099/0022-1317-25-2-187
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