Kinetics of Insertion and Folding of Outer Membrane Proteins by Gel Electrophoresis

2019 ◽  
pp. 145-162 ◽  
Author(s):  
Andre Schüßler ◽  
Sascha Herwig ◽  
Jörg H. Kleinschmidt
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Gel Electrophoresis ◽  
Outer Membrane Proteins ◽  
Kinetics Of

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 Biochemical Analysis of Interactions between Outer Membrane Proteins That Contribute to Starch Utilization byBacteroides thetaiotaomicron

2001 ◽  
Vol 183 (24) ◽  
pp. 7224-7230 ◽  
Author(s):  
Kyu Hong Cho ◽  
Abigail A. Salyers
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Gel Electrophoresis ◽  
Biochemical Analysis ◽  
Outer Membrane Proteins ◽  
Proteinase K ◽  
Cross Linking ◽  
Early Step ◽  
Bacterial Surface ◽  
Starch Utilization

ABSTRACT An early step in the utilization of starch by Bacteroides thetaiotaomicron is the binding of starch to the bacterial surface. Four starch-associated outer membrane proteins of B. thetaiotaomicron that have no starch-degrading activity have been identified. Two of these, SusC and SusD, have been shown by genetic analysis to be required for starch binding. In this study, we provide the first biochemical evidence that these two proteins interact physically with each other. Both formaldehyde cross-linking and nondenaturing gel electrophoresis experiments showed that SusC and SusD interact to form a complex. Two other proteins encoded by genes in the same operon, SusE and SusF, proved not to be essential for starch utilization and actually decreased starch binding when they were present along with SusC and SusD. Consistent with this, nondenaturing gel analysis revealed that in a strain producing SusC, SusD, and SusE, the SusCD complex was partially destabilized. The strain producing SusC, SusD, and SusE also grew more slowly on starch than a strain producing SusC, SusD, SusE, and SusF (μmax, 0.29 and 0.37/h, respectively). Thus, SusE appears to interact with the SusCD complex. SusE also interacts with SusF, because SusE was less susceptible to proteinase K digestion when SusF was present, and nondenaturing gel analysis detected a complex formed by these two proteins. Our results indicate that SusC, SusD, SusE, and SusF form a protein complex in the outer membrane but that SusE and SusF are dispensable members of this complex.

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