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. 1972 Mar;127(1):167–178. doi: 10.1042/bj1270167

The amino acid sequence of the B-protein of bacteriophage ZJ-2

D T Snell 1, R E Offord 1
PMCID: PMC1178571  PMID: 5073740

Abstract

1. Bacteriophage ZJ-2 is a filamentous male-specific coliphage. Methods are given for its preparation and separation into nucleic acid and the major coat-protein component (B-protein). 2. The determination of the amino acid sequence of the B-protein of bacteriophage ZJ-2 is described. The principal features of this aspect of the work were the special procedures dictated by the insolubility of the protein and the extreme insolubility of its fragments. The sequence is compared with that obtained by other workers for the coat protein of the related bacteriophage fd.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Asbeck F., Beyreuther K., Köhler H., von Wettstein G., Braunitzer G. Virusproteine, IV. Die Konstitution des Hüllproteins des Phagen fd. Hoppe Seylers Z Physiol Chem. 1969 Sep;350(9):1047–1066. [PubMed] [Google Scholar]
  2. BRADLEY D. E. THE STRUCTURE OF SOME BACTERIOPHAGES ASSOCIATED WITH MALE STRAINS OF ESCHERICHIA COLI. J Gen Microbiol. 1964 Jun;35:471–482. doi: 10.1099/00221287-35-3-471. [DOI] [PubMed] [Google Scholar]
  3. Braunitzer G., Asbeck F., Beyreuther K., Kohler H., von Wettstein G. Die Konstitution des Hüllproteins des Bakteriophagen fd. Hoppe Seylers Z Physiol Chem. 1967 Dec;348(12):1689–1690. [PubMed] [Google Scholar]
  4. Dixon H. B., Perham R. N. Reversible blocking of amino groups with citraconic anhydride. Biochem J. 1968 Sep;109(2):312–314. doi: 10.1042/bj1090312. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dunker A. K., Rueckert R. R. Observations on molecular weight determinations on polyacrylamide gel. J Biol Chem. 1969 Sep 25;244(18):5074–5080. [PubMed] [Google Scholar]
  6. GRAY W. R., HARTLEY B. S. THE STRUCTURE OF A CHYMOTRYPTIC PEPTIDE FROM PSEUDOMONAS CYTOCHROME C-551. Biochem J. 1963 Nov;89:379–380. doi: 10.1042/bj0890379. [DOI] [PubMed] [Google Scholar]
  7. Gonzalez G., Offord R. E. The subunit structure of prealbumin. Biochem J. 1971 Nov;125(1):309–317. doi: 10.1042/bj1250309. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. HOFFMANN BERLING H., MAZE R. RELEASE OF MALE-SPECIFIC BACTERIOPHAGES FROM SURVIVING HOST BACTERIA. Virology. 1964 Mar;22:305–313. doi: 10.1016/0042-6822(64)90021-2. [DOI] [PubMed] [Google Scholar]
  10. HOFSCHNEIDER P. H., PREUSS A. M 13 BACTERIOPHAGE LIBERATION FROM INTACT BACTERIA AS REVEALED BY ELECTRON MICROSCOPY. J Mol Biol. 1963 Oct;7:450–451. doi: 10.1016/s0022-2836(63)80038-8. [DOI] [PubMed] [Google Scholar]
  11. Henry T. J., Pratt D. The proteins of bacteriophage M13. Proc Natl Acad Sci U S A. 1969 Mar;62(3):800–807. doi: 10.1073/pnas.62.3.800. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hobom G., Braunitzer G. Isolierung von Mutanten des Phagen fd mit proteinchemischen Methoden. Hoppe Seylers Z Physiol Chem. 1967 Jul;348(7):783–796. [PubMed] [Google Scholar]
  13. Knippers R., Hoffmann-Berling H. A coat protein from bacteriophage fd. I. Hydrodynamic measurements and biological characterization. J Mol Biol. 1966 Nov 14;21(2):281–292. doi: 10.1016/0022-2836(66)90099-4. [DOI] [PubMed] [Google Scholar]
  14. LOEB T. Isolation of a bacteriophage specific for the F plus and Hfr mating types of Escherichia coli K-12. Science. 1960 Mar 25;131(3404):932–933. doi: 10.1126/science.131.3404.932. [DOI] [PubMed] [Google Scholar]
  15. Marvin D. A., Hohn B. Filamentous bacterial viruses. Bacteriol Rev. 1969 Jun;33(2):172–209. doi: 10.1128/br.33.2.172-209.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. NAUGHTON M. A., SANGER F., HARTLEY B. S., SHAW D. C. The amino acid sequence around the reactive serine residue of some proteolytic enzymes. Biochem J. 1960 Oct;77:149–163. doi: 10.1042/bj0770149. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Offord R. E. Electrophoretic mobilities of peptides on paper and their use in the determination of amide groups. Nature. 1966 Aug 6;211(5049):591–593. doi: 10.1038/211591a0. [DOI] [PubMed] [Google Scholar]
  18. Rossomando E. F., Zinder N. D. Studies on the bacteriophage fl. I. Alkali-induced disassembly of the phage into DNA and protein. J Mol Biol. 1968 Sep 28;36(3):387–399. doi: 10.1016/0022-2836(68)90163-0. [DOI] [PubMed] [Google Scholar]
  19. WALEY S. G., WATSON J. The action of trypsin on polylysine. Biochem J. 1953 Sep;55(2):328–337. doi: 10.1042/bj0550328. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Williams J. G., Gratzer W. B. Limitations of the detergent-polyacrylamide gel electrophoresis method for molecular weight determination of proteins. J Chromatogr. 1971 Apr 22;57(1):121–125. doi: 10.1016/0021-9673(71)80013-4. [DOI] [PubMed] [Google Scholar]
  21. Woods K. R., Wang K. T. Separation of dansyl-amino acids by polyamide layer chromatography. Biochim Biophys Acta. 1967 Feb 21;133(2):369–370. doi: 10.1016/0005-2795(67)90078-5. [DOI] [PubMed] [Google Scholar]

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