Electrogenic Bromosulfalein Transport in Isolated Membrane Vesicles: Implementation in Both Animal and Plant Preparations for the Study of Flavonoid Transporters

2010 ◽  
pp. 307-335 ◽  
Author(s):  
Sabina Passamonti ◽  
Federica Tramer ◽  
Elisa Petrussa ◽  
Enrico Braidot ◽  
Angelo Vianello
Keyword(s):  
Membrane Vesicles ◽  
Isolated Membrane Vesicles

Rotavirus interaction with isolated membrane vesicles.

1994 ◽  
Vol 68 (6) ◽  
pp. 4009-4016 ◽  
Author(s):  
M C Ruiz ◽  
S R Alonso-Torre ◽  
A Charpilienne ◽  
M Vasseur ◽  
F Michelangeli ◽  
...  
Keyword(s):  
Membrane Vesicles ◽  
Isolated Membrane Vesicles

Use of Isolated Membrane Vesicles in Transport Studies

Transport ◽  
1975 ◽  
pp. 117-162 ◽  
Author(s):  
Joy Hochstadt ◽  
Dennis C. Quinlan ◽  
Richard L. Rader ◽  
Chien-Chung Li ◽  
Diana Dowd
Keyword(s):  
Membrane Vesicles ◽  
Transport Studies ◽  
Isolated Membrane Vesicles

Passive diffusion of nucleosides into Micrococcus sodonensis membrane vesicles

1980 ◽  
Vol 58 (6) ◽  
pp. 457-460 ◽  
Author(s):  
M. A. Pickard
Keyword(s):  
Energy Source ◽  
Membrane Vesicles ◽  
Passive Diffusion ◽  
Membrane Bound ◽  
Nucleoside Uptake ◽  
Membrane Bound Enzymes ◽  
Isolated Membrane Vesicles

Nucleoside entry into isolated membrane vesicles of Micrococcus sodonensis (luteus) was studied using 14C-labelled nucleosides: adenosine, inosine, cytidine, uridine, guanosine, and thymidine. All nucleosides were recovered unmetabolized from the vesicles except adenosine and cytidine which were partly deaminated by membrane-bound enzymes. Vesicle preparations actively transported proline but no energy source was found capable of supporting concentrative nucleoside uptake. The entry of nucleosides into M. sodonensis vesicles was not saturable, nor was there competition between the nucleosides studied for entry. It was concluded that nucleoside entry into M. sodonensis vesicles occurs by passive diffusion.

scholarly journals Biochemical Characterization of the C4-Dicarboxylate Transporter DctA from Bacillus subtilis

2010 ◽  
Vol 192 (11) ◽  
pp. 2900-2907 ◽  
Author(s):  
Maarten Groeneveld ◽  
Ruud G. J. Detert Oude Weme ◽  
Ria H. Duurkens ◽  
Dirk Jan Slotboom
Keyword(s):  
Bacillus Subtilis ◽  
Biochemical Characterization ◽  
Krebs Cycle ◽  
Membrane Vesicles ◽  
Positive Bacterium ◽  
Proton Symport ◽  
Negative Membrane Potential ◽  
Isolated Membrane Vesicles

ABSTRACT Bacterial secondary transporters of the DctA family mediate ion-coupled uptake of C4-dicarboxylates. Here, we have expressed the DctA homologue from Bacillus subtilis in the Gram-positive bacterium Lactococcus lactis. Transport of dicarboxylates in vitro in isolated membrane vesicles was assayed. We determined the substrate specificity, the type of cotransported ions, the electrogenic nature of transport, and the pH and temperature dependence patterns. DctA was found to catalyze proton-coupled symport of the four C4-dicarboxylates from the Krebs cycle (succinate, fumurate, malate, and oxaloacetate) but not of other mono- and dicarboxylates. Because (i) succinate-proton symport was electrogenic (stimulated by an internal negative membrane potential) and (ii) the divalent anionic form of succinate was recognized by DctA, at least three protons must be cotransported with succinate. The results were interpreted in the light of the crystal structure of the homologous aspartate transporter GltPh from Pyrococcus horikoshii.

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