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. 1974 Jan;13(1):155–165. doi: 10.1128/jvi.13.1.155-165.1974

Proteins Specified by Herpes Simplex Virus X. Staining and Radiolabeling Properties of B Capsid and Virion Proteins in Polyacrylamide Gels

Wade Gibson 1, Bernard Roizman 1
PMCID: PMC355270  PMID: 4129836

Abstract

Analyses of the structural proteins of herpes simplex virions and of capsids containing viral DNA (B capsids), after electrophoresis in polyacrylamide gels, revealed considerable variability in their properties with respect to: (i) retention of Coomassie brilliant blue (CBB) and fast green stains during destaining, (ii) relative optical absorbance of the CBB-protein complex at different wavelengths, (iii) relative efficiency with which 14C-amino acids are incorporated during early and late periods of the infection cycle, and (iv) capacity to be phosphorylated in vivo. In addition, it was found that protein 22a of B capsids, which does not have an electrophoretically identical counterpart in virions, shares a relatively unique set of staining and radiolabeling properties with virion protein 22, which has a slightly more rapid electrophoretic mobility in sodium dodecyl sulfate-polyacrylamide gels.

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Selected References

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  1. Anderson C. W., Baum P. R., Gesteland R. F. Processing of adenovirus 2-induced proteins. J Virol. 1973 Aug;12(2):241–252. doi: 10.1128/jvi.12.2.241-252.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Anker H. S. A solubilizable acrylamide gel for electrophoresis. FEBS Lett. 1970 Apr 16;7(3):293–293. doi: 10.1016/0014-5793(70)80185-5. [DOI] [PubMed] [Google Scholar]
  3. Clayton R. K., Haselkorn R. Protein components of bacterial photosynthetic membranes. J Mol Biol. 1972 Jul 14;68(1):97–105. doi: 10.1016/0022-2836(72)90265-3. [DOI] [PubMed] [Google Scholar]
  4. Ejercito P. M., Kieff E. D., Roizman B. Characterization of herpes simplex virus strains differing in their effects on social behaviour of infected cells. J Gen Virol. 1968 May;2(3):357–364. doi: 10.1099/0022-1317-2-3-357. [DOI] [PubMed] [Google Scholar]
  5. Fairbanks G., Jr, Levinthal C., Reeder R. H. Analysis of C14-labeled proteins by disc electrophoresis. Biochem Biophys Res Commun. 1965 Aug 16;20(4):393–399. doi: 10.1016/0006-291x(65)90589-9. [DOI] [PubMed] [Google Scholar]
  6. Fairbanks G., Steck T. L., Wallach D. F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606–2617. doi: 10.1021/bi00789a030. [DOI] [PubMed] [Google Scholar]
  7. Gibson W., Roizman B. Proteins specified by herpes simplex virus. 8. Characterization and composition of multiple capsid forms of subtypes 1 and 2. J Virol. 1972 Nov;10(5):1044–1052. doi: 10.1128/jvi.10.5.1044-1052.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gorovsky M. A., Carlson K., Rosenbaum J. L. Simple method for quantitive densitometry of polyacrylamide gels using fast green. Anal Biochem. 1970 Jun;35(2):359–370. doi: 10.1016/0003-2697(70)90196-x. [DOI] [PubMed] [Google Scholar]
  9. Heine J. W., Spear P. G., Roizman B. Proteins specified by herpes simplex virus. VI. Viral proteins in the plasma membrane. J Virol. 1972 Mar;9(3):431–439. doi: 10.1128/jvi.9.3.431-439.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Keller J. M., Spear P. G., Roizman B. Proteins specified by herpes simplex virus. 3. Viruses differing in their effects on the social behavior of infected cells specify different membrane glycoproteins. Proc Natl Acad Sci U S A. 1970 Apr;65(4):865–871. doi: 10.1073/pnas.65.4.865. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kieff E. D., Bachenheimer S. L., Roizman B. Size, composition, and structure of the deoxyribonucleic acid of herpes simplex virus subtypes 1 and 2. J Virol. 1971 Aug;8(2):125–132. doi: 10.1128/jvi.8.2.125-132.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  13. Randall C. C., Rogers H. W., Downer D. N., Gentry G. A. Protein kinase activity in equine herpesvirus. J Virol. 1972 Feb;9(2):216–222. doi: 10.1128/jvi.9.2.216-222.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Rubenstein A. S., Gravell M., Darlington R. Protein kinase in enveloped herpes simplex virions. Virology. 1972 Oct;50(1):287–290. doi: 10.1016/0042-6822(72)90374-1. [DOI] [PubMed] [Google Scholar]
  15. Russell W. C., Shekel J. J., Machado R., Pereira H. G. Phosphorylated polypeptides in adenovirus-infected cells. Virology. 1972 Dec;50(3):931–934. doi: 10.1016/0042-6822(72)90450-3. [DOI] [PubMed] [Google Scholar]
  16. Sarov I., Joklik W. K. Isolation and characterization of intermediates in vaccinia virus morphogenesis. Virology. 1973 Mar;52(1):223–233. doi: 10.1016/0042-6822(73)90411-x. [DOI] [PubMed] [Google Scholar]
  17. Showe M. K., Black L. W. Assembly core of bacteriophage T4: an intermediate in head formation. Nat New Biol. 1973 Mar 21;242(116):70–75. doi: 10.1038/newbio242070a0. [DOI] [PubMed] [Google Scholar]
  18. Tan K. B., Sokol F. Structural proteins of simian virus 40: phosphoproteins. J Virol. 1972 Nov;10(5):985–994. doi: 10.1128/jvi.10.5.985-994.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]

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