Results 11 to 20 of about 79 (69)

The Na+ and K+ transport deficiency of an E. coli mutant lacking the NhaA and NhaB proteins is apparent and caused by impaired osmoregulation [PDF]

open access: yes, 1998
Cells of the E. coli mutant EP432, which lacks the two Na+/H+ antiporters, NhaA and NhaB, have been reported to have an impaired sodium transport activity (Harel-Bronstein et al. (1995) J. Biol. Chem. 270, 3816–3822). Here we report that active transport
Michael I Verkhovsky   +7 more
core   +1 more source

Functional characterization of a NapA Na(+)/H(+) antiporter from Thermus thermophilus. [PDF]

open access: yes, 2007
Na(+)/H(+) antiporters are ubiquitous membrane proteins and play an important role in cell homeostasis. We amplified a gene encoding a member of the monovalent cation:proton antiporter-2 (CPA2) family (TC 2.A.37) from the Thermus thermophilus genome and ...
Furrer, E M   +7 more
core   +1 more source

Calcium transport mediated by NhaA, a Na+/H+ antiporter from Escherichia coli [PDF]

open access: yes, 1993
In everted membrane vesicles of E. coli strain EP432/pGM42, which has only one Na+/H+ antiporter (NhaA), external CaC4 inhibits dissipation of the respiration-dependent ΔpH in response to the addition of NaCl at pH 7.5, and decreases equilibrium ...
P.A. Dibrov, Dibrov, P.A.
core   +1 more source

Molecular characterization of PeNhaD1: the first member of the NhaD Na+/H+ antiporter family of plant origin

open access: yes, 2005
PeNhaD1 encodes a putative Na+/H+ antiporter from the salt-resistant tree Populus euphratica. It is the first characterization of a member of the NhaD type ion transporter family of plant origin.
Brosché, Mikael   +6 more
core   +1 more source

A167P NhaA mutant growth and expression.

open access: yes, 2014
(A) The double mutant A167P (TM V)-N359D (TM XII) and the previously [24] isolated mutant F267C (TM IX) are shown in red (ball and stick) on the NhaA structure without TM I, for clarity (ribbon presentation by PyMol). Asp163 and Asp164 are shown in black
Miyer Patino-Ruiz (546856)   +6 more
core   +1 more source

Na+ translocation by complex I (NADH:quinone oxidoreductase) of Escherichia coli.

open access: yes, 2000
Following on from our previous discovery of Na+ pumping by the NADH:ubiquinone oxidoreductase (complex I) of Klebsiella pneumoniae, we show here that complex I from Escherichia coli is a Na+ pump as well.
Schmid C   +3 more
core   +1 more source

pH dependence of the Na+, Li+/H+ antiporter activity in everted membrane vesicles of variant A167P.

open access: yes, 2014
Everted membrane vesicles were prepared from EP432 cells grown in LBK (pH 7) and expressing WT (□) or A167P (Δ). The Na+/H+ and Li+/H+ antiporter activity was determined in the presence of 10 mM NaCl (filled symbols) or 10 mM LiCl (open symbols) at the ...
Miyer Patino-Ruiz (546856)   +6 more
core   +1 more source

Expression level, growth phenotype and Na+/H+ antiporter activity of variant A167P.

open access: yes, 2014
aFor characterization of variant A167P, the E coli KNabc (lines 1–4) and E coli EP432 (lines 5–9) cells were transformed with plasmids expressing the indicated variants.
Miyer Patino-Ruiz (546856)   +6 more
core   +1 more source

Oligomerization of NhaA, the Na+/H+ Antiporter of Escherichia coli in the Membrane and Its Functional and Structural Consequences

open access: yes, 2001
Recently, a two-dimensional crystal structure of NhaA, the Na+/H+ antiporter of Escherichia coli has been obtained [Williams, K. A., Kaufer, U. G., Padan, E., Schuldiner, S. and Kühlbrandt, W. (1999) EMBO J., 18, 3558−3563]. In these crystals NhaA exists
Padan, E.   +3 more
core   +1 more source

Na+/H+ antiporter activity of variant A167P in isolated everted membrane vesicles.

open access: yes, 2014
For measurement of the Na+/H+ antiporter activity at the indicated pHs, E. coli EP432/A167P cells expressing variant A167P (A and B) or the wild type (C and D) were grown in LBK (pH 7.0) and everted membrane vesicles were isolated.
Miyer Patino-Ruiz (546856)   +6 more
core   +1 more source

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