Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1979 Dec;140(3):1120–1122. doi: 10.1128/jb.140.3.1120-1122.1979

Lipolytic activity copurified with the outer membrane of Serratia marcescens.

K B Heller
PMCID: PMC216763  PMID: 230176

Abstract

Lipase, nuclease, and protease activities could be shown primarily with the purified outer membrane fraction from Serratia marcescens. These activities increased and decreased in the different compartments dependent on the growth phase of the cell culture. Penicillin-hydrolyzing activity was exclusively demonstrated with the outer membrane fraction.

Full text

PDF
1120

Selected References

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

  1. Aiyappa P. S., Harris J. O. The extracellular metalloprotease of Serratia marcescens: I. Purification and characterization. Mol Cell Biochem. 1976 Nov 30;13(2):95–100. doi: 10.1007/BF01837059. [DOI] [PubMed] [Google Scholar]
  2. 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]
  3. DiRienzo J. M., Nakamura K., Inouye M. The outer membrane proteins of Gram-negative bacteria: biosynthesis, assembly, and functions. Annu Rev Biochem. 1978;47:481–532. doi: 10.1146/annurev.bi.47.070178.002405. [DOI] [PubMed] [Google Scholar]
  4. Eaves G. N., Jeffries C. D. ISOLATION AND PROPERTIES OF AN EXOCELLULAR NUCLEASE OF SERRATIA MARCESCENS. J Bacteriol. 1963 Feb;85(2):273–278. doi: 10.1128/jb.85.2.273-278.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. MacGregor C. H., Bishop C. W., Blech J. E. Localization of proteolytic activity in the outer membrane of Escherichia coli. J Bacteriol. 1979 Jan;137(1):574–583. doi: 10.1128/jb.137.1.574-583.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. NOVICK R. P. Micro-iodometric assay for penicillinase. Biochem J. 1962 May;83:236–240. doi: 10.1042/bj0830236. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Osborn M. J., Gander J. E., Parisi E., Carson J. Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane. J Biol Chem. 1972 Jun 25;247(12):3962–3972. [PubMed] [Google Scholar]
  8. Spratt B. G. Escherichia coli resistance to beta-lactam antibiotics through a decrease in the affinity of a target for lethality. Nature. 1978 Aug 17;274(5672):713–715. doi: 10.1038/274713a0. [DOI] [PubMed] [Google Scholar]
  9. 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]
  10. Winkler U. K., Stuckmann M. Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens. J Bacteriol. 1979 Jun;138(3):663–670. doi: 10.1128/jb.138.3.663-670.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. 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]
  12. Wöhner G., Wöber G. Pullulanase, an enzyme of starch catabolism, is associated with the outer membrane of Klebsiella. Arch Microbiol. 1978 Mar;116(3):303–310. doi: 10.1007/BF00417856. [DOI] [PubMed] [Google Scholar]

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

RESOURCES