Contractile-tailed bacteriophages adsorb toEscherichia coliO128ab lipopolysaccharide that is altered by large plasmids to provide receptors and lipopolysaccharide heterogeneity within the serogroup

1995 ◽  
Vol 41 (2) ◽  
pp. 163-169
Author(s):  
M. L. Kalmokofff ◽  
D. E. Bradley
Keyword(s):  
Escherichia Coli ◽  
Silver Staining ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Coli Strain ◽  
Polyacrylamide Gel ◽  
Clinical Isolates ◽  
Side Chains ◽  
O Antigen ◽  
Large Plasmids

The verotoxigenic Escherichia coli strain H.I.8 (originally O128:B12, now not typeable) contained a ColB+M plasmid and two morphologically identical temperate bacteriophages (HI8A and HI8B). Both phages were O128ab specific, using the lipopolysaccharide O side chains of susceptible clinical isolates as receptors. SDS polyacrylamide gel electrophoresis with silver staining of O128ab lipopolysaccharide revealed four distinct types of ladder with different interband spacings. No specificity was found between ladder type and sensitivity to either phage. One of the numerous large plasmids present in O128ab isolates was found to modify the structure of the lipopolysaccharide O side chains to provide phage receptors.Key words: bacteriophage, plasmid, lipopolysaccharide, O antigen.

Silver staining for proteins in SDS-polyacrylamide gel electrophoresis.

1986 ◽  
Vol 30 (3) ◽  
pp. 229-238 ◽  
Author(s):  
Tsutomu Inoue ◽  
Hiroaki Asaga ◽  
Mayumi Tamura
Keyword(s):  
Silver Staining ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel

scholarly journals Reductive alkylation of ribosomes as a probe to the topography of ribosomal proteins*

1974 ◽  
Vol 143 (3) ◽  
pp. 607-612 ◽  
Author(s):  
Graham Moore ◽  
Robert R. Crichton
Keyword(s):  
Escherichia Coli ◽  
Protein Complex ◽  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Two Dimensional ◽  
Reductive Alkylation ◽  
Lysine Residues

Escherichia coli ribosomes were treated with a number of different aldehydes of various sizes in the presence of NaBH4. After incorporation of either 3H or 14C, the ribosomal proteins were separated by two-dimensional polyacrylamide-gel electrophoresis and the extent of alkylation of the lysine residues in each protein was measured. The same pattern of alkylation was observed with the four reagents used, namely formaldehyde, acetone, benzaldehyde and 3,4,5-trimethoxybenzaldehyde. Every protein in 30S and 50S subunits was modified, although there was considerable variation in the degree of alkylation of individual proteins. A topographical classification of ribosomal proteins is presented, based on the degree of exposure of lysine residues. The data indicate that every protein of the ribosome has at least one lysine residue exposed at or near the surface of the ribonucleo-protein complex.

The influence of proteins on silver staining of nucleic acids following polyacrylamide gel electrophoresis

1995 ◽  
Vol 16 (1) ◽  
pp. 903-904 ◽  
Author(s):  
Friederike Hilbert ◽  
Burkhard Mayr ◽  
Fritz Lackner ◽  
Friedrich Bauer
Keyword(s):  
Nucleic Acids ◽  
Silver Staining ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel
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