Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1979 Jan;137(1):670–672. doi: 10.1128/jb.137.1.670-672.1979

Outer membrane of Serratia marcescens: apparent molecular weights of heat-modifiable proteins in gels with different acrylamide concentrations.

K B Heller
PMCID: PMC218500  PMID: 368037

Abstract

The major proteins from the outer membrane of Serratia marcescens SM-6 are heat modifiable. The analysis of their apparent molecular weights in gels with different concentrations of acrylamide and the results obtained by radioactive labeling indicate that the major proteins are covalently linked to carbohydrate moieties.

Full text

PDF
670

Images in this article

671Image
on p.671

Selected References

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

  1. Bassford P. J., Jr, Diedrich D. L., Schnaitman C. L., Reeves P. Outer membrane proteins of Escherichia coli. VI. Protein alteration in bacteriophage-resistant mutants. J Bacteriol. 1977 Aug;131(2):608–622. doi: 10.1128/jb.131.2.608-622.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Braun V. Covalent lipoprotein from the outer membrane of Escherichia coli. Biochim Biophys Acta. 1975 Oct 31;415(3):335–377. doi: 10.1016/0304-4157(75)90013-1. [DOI] [PubMed] [Google Scholar]
  3. Chai T. J., Foulds J. Escherichia coli K-12 tolF mutants: alterations in protein composition of the outer membrane. J Bacteriol. 1977 May;130(2):781–786. doi: 10.1128/jb.130.2.781-786.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cooksey R. C., Thorne G. M., Farrar W. E., Jr R factor-mediated antibiotic resistance in Serratia marcescens. Antimicrob Agents Chemother. 1976 Jul;10(1):123–127. doi: 10.1128/aac.10.1.123. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Heller K. B. Apparent molecular weights of a heat-modifiable protein from the outer membrane of Escherichia coli in gels with different acrylamide concentrations. J Bacteriol. 1978 Jun;134(3):1181–1183. doi: 10.1128/jb.134.3.1181-1183.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hughes R. C. The complex carbohydrates of mammalian cell surfaces and their biological roles. Essays Biochem. 1975;11:1–36. [PubMed] [Google Scholar]
  7. Leive L. The barrier function of the gram-negative envelope. Ann N Y Acad Sci. 1974 May 10;235(0):109–129. doi: 10.1111/j.1749-6632.1974.tb43261.x. [DOI] [PubMed] [Google Scholar]
  8. Manning P. A., Puspurs A., Reeves P. Outer membrane of Escherichia coli K-12: isolation of mutants with altered protein 3A by using host range mutants of bacteriophage K3. J Bacteriol. 1976 Sep;127(3):1080–1084. doi: 10.1128/jb.127.3.1080-1084.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Pazur J. H., Knull H. R., Simpson D. L. Glycoenzymes: a note on the role for the carbohydrate moieties. Biochem Biophys Res Commun. 1970 Jul 13;40(1):110–116. doi: 10.1016/0006-291x(70)91053-3. [DOI] [PubMed] [Google Scholar]
  10. Randall L. L. Quantitation of the loss of the bacteriophage lambda receptor protein from the outer membrane of lipopolysaccharide-deficient strains of Escherichia coli. J Bacteriol. 1975 Jul;123(1):41–46. doi: 10.1128/jb.123.1.41-46.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Rosenbusch J. P. Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding. J Biol Chem. 1974 Dec 25;249(24):8019–8029. [PubMed] [Google Scholar]
  12. Schnaitman C. A. Protein composition of the cell wall and cytoplasmic membrane of Escherichia coli. J Bacteriol. 1970 Nov;104(2):890–901. doi: 10.1128/jb.104.2.890-901.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Schweizer M., Schwarz H., Sonntag I., Henning U. Mutational change of membrane architecture. Mutants of Escherichia coli K12 missing major proteins of the outer cell envelope membrane. Biochim Biophys Acta. 1976 Oct 19;448(3):474–491. doi: 10.1016/0005-2736(76)90301-1. [DOI] [PubMed] [Google Scholar]
  14. Steven A. C., Heggeler B., Müller R., Kistler J., Rosenbusch J. P. Ultrastructure of a periodic protein layer in the outer membrane of Escherichia coli. J Cell Biol. 1977 Feb;72(2):292–301. doi: 10.1083/jcb.72.2.292. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Timmis K., Winkler U. Isolation of covalently closed circular deoxyribonucleic acid from bacteria which produce exocellular nuclease. J Bacteriol. 1973 Jan;113(1):508–509. doi: 10.1128/jb.113.1.508-509.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Weber D. A., Nadakavukaren M. J., Tsang J. C. Effect of polymyxin B on outer membranes of Serratia marcescens: morphological alterations of the outer membranes and their lipopolysaccharide components. Microbios. 1976;17(68-69):149–161. [PubMed] [Google Scholar]
  17. Winkler U., Heller K. B., Folle B. Pleiotropic consequences of mutations towards antibiotic-hypersensitivity in Serratia marcescens. Arch Microbiol. 1978 Mar;116(3):259–268. doi: 10.1007/BF00417849. [DOI] [PubMed] [Google Scholar]
  18. Yamato I., Futai M., Anraku Y., Nonomura Y. Cytoplasmic membrane vesicles of Escherichia coli. II. Orientation of the vesicles studied by localization of enzymes. J Biochem. 1978 Jan;83(1):117–128. doi: 10.1093/oxfordjournals.jbchem.a131882. [DOI] [PubMed] [Google Scholar]
  19. van Alphen W., Lugtenberg B., Berendsen W. Heptose-deficient mutants of Escherichia coli K12 deficient in up to three major outer membrane proteins. Mol Gen Genet. 1976 Sep 23;147(3):263–269. doi: 10.1007/BF00582877. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES