Abstract
The protein composition of the outer membrane of Salmonella typhimurium has been analyzed by electrophoresis on slabs of sodium dodecyl sulfate-acrylamide gel. This powerful technique allows very high resolution of protein mixtures and has permitted the identification of multiple major protein components of the outer membrane; no evidence for a single major component of molecular weight 44,000 was obtained. These proteins were shown to be decreased in amount in mutants which have defective lipopolysaccharides. Mutants of an apparently new type were also found which contain decreased amounts of the proteins and the parent-like lipopolysaccharide, yet are resistant to a lipopolysaccharide-specific phage, C21. Several outer membrane proteins are insoluble in sodium dodecyl sulfate unless heated at high temperature (above 70 C). A purification procedure based on this property is tentatively suggested.
MeSH Terms
Bacterial Proteins/analysis,isolation & purification
Cell Wall/analysis
Chromatography, Gas
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Glucosamine/analysis
Heptoses/analysis
Hot Temperature
Keto Acids/analysis
Lipopolysaccharides/analysis
Molecular Weight
Mutation
Polysaccharides, Bacterial/analysis
Salmonella typhimurium/analysis,cytology
Solubility
Chemicals
Bacterial Proteins
Heptoses
Keto Acids
Lipopolysaccharides
Polysaccharides, Bacterial
Glucosamine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Ames G F
Spudich E N
Nikaido H
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