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Cited by 271

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Overproduction and purification of a functional Na+/H+ antiporter coded by nhaA (ant) from Escherichia coli

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Taglicht, D., Padan, E., Schuldiner, S.·1991·Journal of Biological Chemistry

Abstract

A Na+/H+ antiporter coded by the nhaA (ant) gene of Escherichia coli has been overproduced and purified. The amino-terminal sequence of the protein has been determined and shown to correlate with initiation at a GUG codon, 75 bases upstream from the previously suggested AUG initiation codon. The purified protein, when reconstituted into proteoliposomes, has Na+/H+ antiport activity. It can mediate sodium uptake when a transmembrane pH gradient is applied. Downhill sodium efflux is shown to be highly dependent on pH and is accelerated by a transmembrane pH gradient. An imposed membrane potential negative inside accelerates Na+ efflux at all pH values tested. These findings suggest that the antiporter is electrogenic both at acid and alkaline pH. The activation at alkaline pH values (2000-fold increase) is consistent with the proposed role of the antiporter in regulation of internal pH at the alkaline pH range.

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Metadata

Authors
Taglicht, D., Padan, E., & Schuldiner, S.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1991-06
Volume
266
Issue
17
Pages
11289-11294
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1541707791
Cited by
271
References
25
FWCI
7.86
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Overproduction and purification of a functional Na+/H+ antiporter coded by nhaA (ant) from Escherichia coli. https://app.cochat.ai/papers/10.1016/s0021-9258(18)99161-1
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Taglicht, D., Padan, E., & Schuldiner, S. (1991). Overproduction and purification of a functional Na+/H+ antiporter coded by nhaA (ant) from Escherichia coli. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)99161-1

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