scholarly journals Two-Dimensional Gel Electrophoresis and Immunoblotting of Campylobacter Outer Membrane Proteins

1987 ◽  
Author(s):  
Bruce E. Dunn ◽  
Martin J. Blaser ◽  
Edward L. Snyder
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Gel Electrophoresis ◽  
Outer Membrane Proteins ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

Outer membrane proteins from Serratia marcescens

1993 ◽  
Vol 39 (1) ◽  
pp. 108-111 ◽  
Author(s):  
Marta Puig ◽  
Carme Fusté ◽  
Miquel Viñas
Keyword(s):  
Membrane Proteins ◽  
Serratia Marcescens ◽  
Outer Membrane ◽  
Nutrient Availability ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Outer Membrane Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cultural Conditions

The outer membrane proteins (OMPs) of several strains of Serratia marcescens have been studied by sodium dodecyl sulphate – urea – polyacrylamide gel electrophoresis. Four major OMPs, named Omp1, Omp2, Omp3, and OmpA (42, 40, 39, and 37 kDa, respectively), have been visualized. The relative proportions of Omp2 and Omp3 depend on cultural conditions (temperature of incubation, osmolarity, and nutrient availability).Key words: Serratia marcescens, outer membrane proteins, porin.

Identification of Campylobacter jejuni and C. coli by gel electrophoresis of the outer membrane proteins.

1989 ◽  
Vol 27 (5) ◽  
pp. 1072-1076 ◽  
Author(s):  
I Derclaye ◽  
I Delor ◽  
M Van Bouchaute ◽  
P Moureau ◽  
G Wauters ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Campylobacter Jejuni ◽  
Gel Electrophoresis ◽  
Outer Membrane Proteins

scholarly journals Fate of Predator and Prey Proteins during Growth of Bdellovibrio bacteriovorus on Escherichia coli and Pseudomonas syringae Prey

2005 ◽  
Vol 187 (1) ◽  
pp. 329-335 ◽  
Author(s):  
Gilli Barel ◽  
Alexandra Sirota ◽  
Hanne Volpin ◽  
Edouard Jurkevitch
Keyword(s):  
Escherichia Coli ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Pseudomonas Syringae ◽  
Outer Membrane Proteins ◽  
Cell Fraction ◽  
Two Dimensional ◽  
Protein Distribution ◽  
Bdellovibrio Bacteriovorus ◽  
Cell Envelopes

ABSTRACT A two-dimensional electrophoretic analysis of protein distribution followed by identification of selected proteins by mass spectrometry was performed on fresh bdellovibrio cultures containing attack phase cells of the predatory bacterium Bdellovibrio bacteriovorus strain 109J-1 and the remains of an Escherichia coli or a Pseudomonas syringae pv. tomato prey. Cleavage of the peptidoglycan-associated outer membrane proteins (OMPs) OmpA in E. coli and OprF in P. syringae occurred in both prey. The tryptic peptides obtained from the cleavage products of OmpA and OprF were all located within the 19-kDa pronase-resistant N-terminal parts of the corresponding proteins. The predator cell fraction was separated from the prey ghosts in fresh bdellovibrio cultures by centrifugation on a Percoll-sucrose cushion. Proteins from each fraction were separated by two-dimensional electrophoresis and identified by mass spectrometric analysis. As no prey OMP could be detected in the predator cell fraction, it was concluded that prey OMPs are not transferred to the predator, as had been suggested previously. However, a protein from the predator was found bound to ghost cell envelopes. This protein may correspond to a protein earlier suggested to be associated with the prey outer or cytoplasmic membranes. Along with recently described polypeptides from B. bacteriovorus strains 100 and 114, it forms a new family of putative outer membrane proteins.

Sign in / Sign up

Export Citation Format

Share Document