Abstract
Polyoma and Shope papilloma viruses were purified and analyzed by chemical and physical methods. Disc electrophoresis of degraded virions indicated the presence, in both cases, of only one major species of polypeptide subunit. The weight of the peptide chain of polyoma virus was estimated in 8 m urea to be about 45,000 avograms, based on the sedimentation rate in a sucrose-urea gradient and the diffusion coefficient estimated from the differential migration in electrophoresis in gels of different pore size. The presence of a minor peptide of smaller size was suggested by carboxyl-terminal and sedimentation analyses. The amino acid composition of polyoma capsid protein was reported. Chemical analyses showed that polyoma virus and Shope papilloma virus contained 16 and 17.5% deoxyribonucleic acid, respectively. Light scattering by the polyoma virion showed it to have a molecular weight of 22 × 106 and a diameter of 54 nm.
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- BARTLETT G. R. Phosphorus assay in column chromatography. J Biol Chem. 1959 Mar;234(3):466–468. [PubMed] [Google Scholar]
- CARLTON B. C., YANOFSKY C. The carboxyl-terminal sequence of the A protein of tryptophan synthetase of Escherichia coli. J Biol Chem. 1963 Feb;238:636–639. [PubMed] [Google Scholar]
- CRAWFORD L. V., CRAWFORD E. M. A COMPARATIVE STUDY OF POLYOMA AND PAPILLOMA VIRUSES. Virology. 1963 Oct;21:258–263. doi: 10.1016/0042-6822(63)90265-4. [DOI] [PubMed] [Google Scholar]
- CRESTFIELD A. M., MOORE S., STEIN W. H. The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J Biol Chem. 1963 Feb;238:622–627. [PubMed] [Google Scholar]
- DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
- DAVISON P. F., FREIFELDER D. The physical properties of T7 bacteriophage. J Mol Biol. 1962 Dec;5:635–642. doi: 10.1016/s0022-2836(62)80091-6. [DOI] [PubMed] [Google Scholar]
- ENGLANDER S. W., EPSTEIN H. T. Optical methods for measuring nucleoprotein and nucleic acid concentrations. Arch Biochem Biophys. 1957 May;68(1):144–149. doi: 10.1016/0003-9861(57)90334-x. [DOI] [PubMed] [Google Scholar]
- Goodwin T. W., Morton R. A. The spectrophotometric determination of tyrosine and tryptophan in proteins. Biochem J. 1946;40(5-6):628–632. doi: 10.1042/bj0400628. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hare J. D., Chan J. C. Role of hydrogen and disulfide bonds in polyoma capsid structure. Virology. 1968 Mar;34(3):481–491. doi: 10.1016/0042-6822(68)90068-8. [DOI] [PubMed] [Google Scholar]
- KLUG A. STRUCTURE OF VIRUSES OF THE PAPILLOMA-POLYOMA TYPE. II. COMMENTS ON OTHER WORK. J Mol Biol. 1965 Feb;11:424–431. doi: 10.1016/s0022-2836(65)80067-5. [DOI] [PubMed] [Google Scholar]
- Kass S. J., Knight C. A. Purification and chemical analysis of Shope papilloma virus. Virology. 1965 Nov;27(3):273–281. doi: 10.1016/0042-6822(65)90106-6. [DOI] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- MARLER E., NELSON C. A., TANFORD C. THE POLYPEPTIDE CHAINS OF RABBIT GAMMA-GLOBULIN AND ITS PAPAIN-CLEAVED FRAGMENTS. Biochemistry. 1964 Feb;3:279–284. doi: 10.1021/bi00890a024. [DOI] [PubMed] [Google Scholar]
- MARTIN R. G., AMES B. N. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J Biol Chem. 1961 May;236:1372–1379. [PubMed] [Google Scholar]
- MCKENZIE H. A., SMITH M. B., WAKE R. G. The denaturation of proteins. I. Sedimentation, diffusion, optiacal rotation, viscosity and gelation in urea solutions of ovalumin and bovine serum albumin. Biochim Biophys Acta. 1963 Feb 5;69:222–239. doi: 10.1016/0006-3002(63)91256-3. [DOI] [PubMed] [Google Scholar]
- Mass M., Fine R., Murakami W. T. Protein composition of polyoma virus. J Mol Biol. 1968 Aug 28;36(1):167–177. doi: 10.1016/0022-2836(68)90227-1. [DOI] [PubMed] [Google Scholar]
- Murakami W. T., Fine R., Harrington M. R., Sassan Z. B. Properties and amino acid composition of polyoma virus purified by zonal ultracentrifugation. J Mol Biol. 1968 Aug 28;36(1):153–166. doi: 10.1016/0022-2836(68)90226-x. [DOI] [PubMed] [Google Scholar]
- ORNSTEIN L. DISC ELECTROPHORESIS. I. BACKGROUND AND THEORY. Ann N Y Acad Sci. 1964 Dec 28;121:321–349. doi: 10.1111/j.1749-6632.1964.tb14207.x. [DOI] [PubMed] [Google Scholar]
- REISFELD R. A., LEWIS U. J., WILLIAMS D. E. Disk electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature. 1962 Jul 21;195:281–283. doi: 10.1038/195281a0. [DOI] [PubMed] [Google Scholar]
- RUECKERT R. R., SCHAEFER W. STUDIES ON THE STRUCTURE OF VIRUSES OF THE COLUMBIA SK GROUP. I. PURIFICATION AND PROPERTIES OF ME-VIRUS GROWN IN EHRLICH ASCITES CELL SUSPENSIONS. Virology. 1965 Jun;26:333–344. doi: 10.1016/0042-6822(65)90281-3. [DOI] [PubMed] [Google Scholar]
- RUECKERT R. R. 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. 1965 Jun;26:345–358. doi: 10.1016/0042-6822(65)90282-5. [DOI] [PubMed] [Google Scholar]
- Thorne H. V., Warden D. Electrophoretic evidence for a single protein component in the capsid of polyoma virus. J Gen Virol. 1967 Jan;1(1):135–137. doi: 10.1099/0022-1317-1-1-135. [DOI] [PubMed] [Google Scholar]
- Vinograd J., Lebowitz J., Radloff R., Watson R., Laipis P. The twisted circular form of polyoma viral DNA. Proc Natl Acad Sci U S A. 1965 May;53(5):1104–1111. doi: 10.1073/pnas.53.5.1104. [DOI] [PMC free article] [PubMed] [Google Scholar]
- WEIL R., VINOGRAD J. THE CYCLIC HELIX AND CYCLIC COIL FORMS OF POLYOMA VIRAL DNA. Proc Natl Acad Sci U S A. 1963 Oct;50:730–738. doi: 10.1073/pnas.50.4.730. [DOI] [PMC free article] [PubMed] [Google Scholar]
- WINOCOUR E. Purification of polyoma virus. Virology. 1963 Feb;19:158–168. doi: 10.1016/0042-6822(63)90005-9. [DOI] [PubMed] [Google Scholar]