Amiloride-sensitive Na+-H+ antiporter in Escherichia coli

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Amiloride-sensitive Na+-H+ antiporter in Escherichia coli.

In everted vesicles of Escherichia coli, delta pH caused by H+ efflux through the Na+/H+ antiporter was measured by using a fluorescent dye. Amiloride inhibited the activity of the Na+/H+ antiporter. Kinetic studies showed that amiloride competed with Na+. The inhibition constant of 40 microM was obtained.

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Physiological role of nhaB, a specific Na+/H+ antiporter in Escherichia coli.

The nhaB gene which codes for Na+/H+ antiporter activity in Escherichia coli was recently cloned (Pinner, E., Padan, E., and Schuldiner, S. (1992) J. Biol. Chem. 267, 11064-11068). In order to elucidate the role of nhaB in Na+ and H+ ions physiology and its interaction with nhaA, we generated mutants in which the chromosomal gene has been inactivated by insertion/deletion. A mutant devoid of bo...

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Cloning, sequencing, and expression of the nhaB gene, encoding a Na+/H+ antiporter in Escherichia coli.

In Escherichia coli, expulsion of sodium ions is driven by proton flux via at least two distinct Na+/H+ antiporters, NhaA and NhaB. When the nhaA gene is deleted from the chromosome, the cell becomes sensitive to high salinity and alkaline pH (Padan, E., Maisler, N., Taglicht, D., Karpel, R., and Schuldiner, S. (1989) J. Biol. Chem. 264, 20297-20302). In the current work we cloned the nhaB gene...

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Multiconformation continuum electrostatics analysis of the NhaA Na+/H+ antiporter of Escherichia coli with functional implications.

Sodium proton antiporters are essential enzymes that catalyze the exchange of sodium ions for protons across biological membranes. Protonations and deprotonations of individual amino acid residues and of clusters formed by these residues play an important role in activating these enzymes and in the mechanism of transport. We have used multiconformation continuum electrostatics method to investi...

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Topological analysis of NhaA, a Na+/H+ antiporter from Escherichia coli.

Analysis of the hydropathic profile of the amino acid sequence of NhaA, a Na+/H+ antiporter from Escherichia coli has previously suggested the existence of 11 putative transmembrane segments (Taglicht, D., Padan, E., and Schuldiner, S. (1991) J. Biol. Chem. 266, 11289-11294). In the present work to test the location of the C terminus, right-side-out and inside-out membrane vesicles were digeste...

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ژورنال

عنوان ژورنال: Journal of Bacteriology

سال: 1985

ISSN: 0021-9193,1098-5530

DOI: 10.1128/jb.163.1.395-397.1985