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1.
FIG. 3.

FIG. 3. From: Catalytic Properties of Staphylococcus aureus and Bacillus Members of the Secondary Cation/Proton Antiporter-3 (Mrp) Family Are Revealed by an Optimized Assay in an Escherichia coli Host .

Na+/H+ antiport activity of Mrp antiporters as a function of pH. The assay protocol was as described in the legend to Fig. 2, with the pH of the buffers adjusted to the values indicated. The data shown are for assays with 2.5 mM NaCl. The error bars indicate standard deviations from duplicate assays from three independent experiments.

Talia H. Swartz, et al. J Bacteriol. 2007 April;189(8):3081-3090.
2.
FIG. 5.

FIG. 5. From: Catalytic Properties of Staphylococcus aureus and Bacillus Members of the Secondary Cation/Proton Antiporter-3 (Mrp) Family Are Revealed by an Optimized Assay in an Escherichia coli Host .

NhaA-dependent effects on ΔΨ generation and Na+-dependent ΔΨ consumption. Fluorescence-based assays of everted membrane vesicles from control and NhaA transformants of E. coli EP432 were performed exactly as described in the legend to Fig. 4 except that the vector was pBR322 instead of pGEM3Z(f+) and only ΔΨ generation was assessed in the experiments shown in panel A, whereas both ΔΨ generation and Na+-dependent ΔΨ consumption were assessed in those shown in panel B. The traces shown are representative of at least three independent experiments. CCCP, carbonyl cyanide m-chlorophenylhydrazone.

Talia H. Swartz, et al. J Bacteriol. 2007 April;189(8):3081-3090.
3.
FIG. 6.

FIG. 6. From: Catalytic Properties of Staphylococcus aureus and Bacillus Members of the Secondary Cation/Proton Antiporter-3 (Mrp) Family Are Revealed by an Optimized Assay in an Escherichia coli Host .

Sodium dithionite reduced-minus-air-oxidized spectra of everted membrane vesicles of control or Mrp-Mnh-expressing E. coli EP432. Everted membrane vesicles (2 mg/ml) were suspended in 50 mM Tricine (pH 8.0) containing 0.1% dodecyl maltoside. Dithionite was added, and spectra were recorded after 1 min of incubation at room temperature. The traces shown are representative of at least three independent experiments. The peak at 560 nm corresponds to cytochrome b, and the peak at 630 nm corresponds to cytochrome d.

Talia H. Swartz, et al. J Bacteriol. 2007 April;189(8):3081-3090.
4.
FIG. 2.

FIG. 2. From: Catalytic Properties of Staphylococcus aureus and Bacillus Members of the Secondary Cation/Proton Antiporter-3 (Mrp) Family Are Revealed by an Optimized Assay in an Escherichia coli Host .

Na+/H+ antiport activity of Mrp antiporters as a function of cation concentration at pH 8.5. Fluorescence-based assays of the Na+/H+ antiport activities of the Mrp antiporters in E. coli EP432 vesicles were conducted at pH 8.5 over a range of concentrations of added NaCl; the Michaelis-Menten plot is shown, and a reciprocal plot is shown as an inset in each panel. The assay protocol was identical to that described in Table 2, footnote a. The standard deviations of the values, which are derived from duplicate assays in at least three independent experiments, were less than 10% of the mean values.

Talia H. Swartz, et al. J Bacteriol. 2007 April;189(8):3081-3090.
5.
FIG. 1.

FIG. 1. From: Catalytic Properties of Staphylococcus aureus and Bacillus Members of the Secondary Cation/Proton Antiporter-3 (Mrp) Family Are Revealed by an Optimized Assay in an Escherichia coli Host .

Effect of NaCl concentration and pH on the growth of E. coli EP432 transformants of Mrp-Mnh antiporters. (A) Transformants with empty vector [pGEM-3Zf(+)], or expressing the Mrp operons from B. subtilis, B. pseudofirmus OF4, or S. aureus were grown on LBK medium, pH 7.5, containing added NaCl at the indicated concentrations. (B) LBK with no added NaCl was adjusted to the pH values indicated. The LBK contained approximately 12 mM contaminating Na+ (62). Cells were grown overnight for 16 h at 37°C, with shaking, after which the A600 of the cultures was measured. The error bars indicate standard deviations from duplicate cultures in three independent experiments.

Talia H. Swartz, et al. J Bacteriol. 2007 April;189(8):3081-3090.
6.
FIG. 4.

FIG. 4. From: Catalytic Properties of Staphylococcus aureus and Bacillus Members of the Secondary Cation/Proton Antiporter-3 (Mrp) Family Are Revealed by an Optimized Assay in an Escherichia coli Host .

Electrogenicity of Mrp-dependent Na+/H+ antiport. Fluorescence-based assays of everted membrane vesicles from the control, MrpBpOF4, and Mnh transformants of E. coli EP432 were performed in reaction mixtures containing 200 μg vesicle protein/ml in a total of 2 ml. The reaction mixtures contained 50 mM BTP-sulfate, 5 mM MgSO4, 200 mM K2SO4, and 1 μM nigericin at pH 7.5, plus 1 μM oxonol VI. To initiate respiration, 1 mM Tris-NADH was added at the first arrow. Once the quenching achieved steady state, 10 mM NaCl was added at the second arrow. The final arrow indicates the addition of 10 μM carbonyl cyanide m-chlorophenylhydrazone (CCCP). The traces shown are representative of at least three independent experiments.

Talia H. Swartz, et al. J Bacteriol. 2007 April;189(8):3081-3090.

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