Isolation of differentiated membrane domains from Escherichia coli and Salmonella typhimurium, including a fraction containing sites between the inner and outer membranes and Murein skeleton of the cell envelope
Abstract
Cell envelopes of Salmonella typhimurium and Escherichia coli were disrupted in a French pressure cell and fractionated by successive cycles of sedimentation and floatation density gradient centrifugation. This permitted the identification and isolation of several membrane fractions in addition to the major inner membrane and murein-outer membrane fractions. One of these fractions (fraction OM/sub L/) accounted for about 10% of the total cell envelope protein, and is likely to include the murein-membrane adhesion zones that are seen in electron micrographs of plasmolyzed cells. Fraction OM/sub L/ contained inner membrane, murein, and outer membrane in an apparently normal configuration, was capable of synthesizing murein from UDP-(/sup 3/H)N-acetylglucosamine and UDP-N-acetylmuramyl-pentapeptide and covalently linking it to the endogenous murein of the preparation. It showed a labeling pattern in (/sup 3/H)galactose pulse-chase experiments that was consistent with its acting as an intermediate in the movement of newly synthesized lipopolysaccharide from inner membrane to outer membrane.
- Publication Date:
- Research Org.:
- Univ. of Connecticut Health Center, Farmington
- OSTI Identifier:
- 5219959
- Resource Type:
- Journal Article
- Journal Name:
- J. Biol. Chem.; (United States)
- Additional Journal Information:
- Journal Volume: 261:1
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; CELL MEMBRANES; BIOCHEMICAL REACTION KINETICS; ESCHERICHIA COLI; SALMONELLA TYPHIMURIUM; EXPERIMENTAL DATA; LIPOPOLYSACCHARIDES; PROTEINS; SEPARATION PROCESSES; TRACER TECHNIQUES; TRITIUM COMPOUNDS; BACTERIA; CARBOHYDRATES; CELL CONSTITUENTS; DATA; INFORMATION; ISOTOPE APPLICATIONS; KINETICS; LABELLED COMPOUNDS; LIPIDS; MEMBRANES; MICROORGANISMS; NUMERICAL DATA; ORGANIC COMPOUNDS; POLYSACCHARIDES; REACTION KINETICS; SACCHARIDES; SALMONELLA; 550201* - Biochemistry- Tracer Techniques; 550701 - Microbiology- Tracer Techniques
Citation Formats
. Isolation of differentiated membrane domains from Escherichia coli and Salmonella typhimurium, including a fraction containing sites between the inner and outer membranes and Murein skeleton of the cell envelope. United States: N. p., 1986.
Web.
. Isolation of differentiated membrane domains from Escherichia coli and Salmonella typhimurium, including a fraction containing sites between the inner and outer membranes and Murein skeleton of the cell envelope. United States.
. 1986.
"Isolation of differentiated membrane domains from Escherichia coli and Salmonella typhimurium, including a fraction containing sites between the inner and outer membranes and Murein skeleton of the cell envelope". United States.
@article{osti_5219959,
title = {Isolation of differentiated membrane domains from Escherichia coli and Salmonella typhimurium, including a fraction containing sites between the inner and outer membranes and Murein skeleton of the cell envelope},
author = {},
abstractNote = {Cell envelopes of Salmonella typhimurium and Escherichia coli were disrupted in a French pressure cell and fractionated by successive cycles of sedimentation and floatation density gradient centrifugation. This permitted the identification and isolation of several membrane fractions in addition to the major inner membrane and murein-outer membrane fractions. One of these fractions (fraction OM/sub L/) accounted for about 10% of the total cell envelope protein, and is likely to include the murein-membrane adhesion zones that are seen in electron micrographs of plasmolyzed cells. Fraction OM/sub L/ contained inner membrane, murein, and outer membrane in an apparently normal configuration, was capable of synthesizing murein from UDP-(/sup 3/H)N-acetylglucosamine and UDP-N-acetylmuramyl-pentapeptide and covalently linking it to the endogenous murein of the preparation. It showed a labeling pattern in (/sup 3/H)galactose pulse-chase experiments that was consistent with its acting as an intermediate in the movement of newly synthesized lipopolysaccharide from inner membrane to outer membrane.},
doi = {},
url = {https://www.osti.gov/biblio/5219959},
journal = {J. Biol. Chem.; (United States)},
number = ,
volume = 261:1,
place = {United States},
year = {Sun Jan 05 00:00:00 EST 1986},
month = {Sun Jan 05 00:00:00 EST 1986}
}