Journal of Bacteriology · 1985 · 177 citations · 27 references
Life SciencesMicrobiologyMolecular BiologyBacteriologyMedical MicrobiologyProtein BiochemistryBacterial ImmunologyBacterial SerologyCapsular PolysaccharidesEscherichia ColiPolyacrylamide Gel ElectrophoresisSodium Dodecyl Sulfate-polyacrylamide Gel Electrophoresis
Lipopolysaccharide from smooth strains of Salmonella typhimurium, Salmonella minnesota, and Escherichia coli O111:B4, O55:B5, and O127:B8 was fractionated by gel filtration chromatography. All lipopolysaccharide samples separated into three major populations. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the fractions from S. typhimurium and S. minnesota indicated that the three peaks were made up of molecules with average O-antigen lengths of (i) 70 or more repeat units, (ii) 30 and 20 repeats units in the samples from S. typhimurium and S. minnesota, respectively, and (iii) 1 repeat unit. In contrast to the Salmonella samples, peak 1 from the E. coli samples was not detected on polyacrylamide gels and lacked detectable phosphate. This high-molecular-weight material had a sugar composition similar to that of O-antigen and was tentatively identified as capsular polysaccharide. Peaks 2 and 3 of the E. coli samples were analogous to those of the Salmonella isolates, containing lipopolysaccharide molecules with averages of 18 and 1 O-antigen repeat units, respectively. These lipopolysaccharide molecules did not completely dissociate during electrophoresis, and multimers were detected as distinct, anomalous, slow-migrating bands. Increasing the concentration of sodium dodecyl sulfate in the gels resulted in the dissociation of these multimers.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
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