Results 201 to 210 of about 8,789 (241)
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Biology of the 2Na+/1H+ antiporter in invertebrates
Journal of Experimental Zoology, 2000The functional expression of membrane transport proteins that are responsible for exchanging sodium and protons is a ubiquitous phenomenon. Among vertebrates the Na+/H+ antiporter occurs in plasma membranes of polarized epithelial cells and non-polarized cells such as red blood cells, muscle cells, and neurons, and in each cell type the transporter ...
G A, Ahearn, P K, Mandal, A, Mandal
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Journal of Biochemistry, 1998
We detected chloramphenicol/H+ antiport activity in membrane vesicles of Escherichia coli and cloned a gene for the antiporter from chromosomal DNA of E. coli. Introduction of the gene into E. coli cells conferred resistance to chloramphenicol and ethidium. A slight increase in resistance to acridine orange was also observed.
T, Mine +4 more
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We detected chloramphenicol/H+ antiport activity in membrane vesicles of Escherichia coli and cloned a gene for the antiporter from chromosomal DNA of E. coli. Introduction of the gene into E. coli cells conferred resistance to chloramphenicol and ethidium. A slight increase in resistance to acridine orange was also observed.
T, Mine +4 more
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Anticipating antiport in P-type ATPases
Trends in Biochemical Sciences, 2008Cation-transporting P-type ATPases show a high degree of structural and functional homology. Nevertheless, for many members of this large family, the molecular mechanism of transport is unclear; namely, whether transport is electrogenic or not and if countertransport is involved remains to be established. In a few well-studied cases such as the Na(+)-K(
Niggli, Verena, Sigel, Erwin
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Structure and mechanism of a glutamate–GABA antiporter
Nature, 2012Food-borne hemorrhagic Escherichia coli, exemplified by the strains O157:H7 and O104:H4 (refs 1, 2), require elaborate acid-resistance systems (ARs) to survive the extremely acidic environment such as the stomach (pH ≈ 2). AR2 expels intracellular protons through the decarboxylation of L-glutamate (Glu) in the cytoplasm and exchange of the reaction ...
Dan, Ma +6 more
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The Tricky Task of Nitrate/Nitrite Antiport
Angewandte Chemie International Edition, 2013Subtle differences: Two recent crystal structures have provided the first insight into nitrate/nitrite exchangers (example shown with bound nitrite), which are crucial to bacterial metabolism. A direct comparison of the structures reveals how the proteins can distinguish between their highly similar substrates and translate this into a conformational ...
Andrade, Susana L. A., Einsle, Oliver
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The Na+/H+ antiport in renal mitochondria
American Journal of Physiology-Cell Physiology, 1995In isolated renal mitochondria, Na+ and Li+ stimulated H+ efflux from the mitochondrial matrix. In submitochondrial particles (SMP), Na+ flux was also coupled to H+ transport in the opposite direction. The overshoot of Na+ uptake in SMP with an outwardly directed H+ gradient indicated that downhill efflux of H+ through the mitochondrial membrane ...
M, Sastrasinh +3 more
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On Bounded Symport/Antiport P Systems
2006We introduce a restricted model of a one-membrane symport/antiport system, called bounded S/A system. We show the following: 1. A language $L \subseteq a_1^* ... a_k^*$ is accepted by a bounded S/A system if and only if it is accepted by a log n space-bounded Turing machine. This holds for both deterministic and nondeterministic versions. 2.
Oscar H. Ibarra, Sara Woodworth
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P Systems with Symport/Antiport and Time
2006We consider symport/antiport P systems using the time as the support for the output of a computation. We describe and study the properties of “timed symport/antiport systems”, showing that this new model of membrane systems based on time has more power/flexibility, and thus allows us to improve previous universality results.
Hitesh Nagda +2 more
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Genetic and Biochemical Characterization of the Na+/H+ Antiporters of Pseudomonas aeruginosa.
Journal of Bacteriology, 2021Ana E Duran-Pinedo +2 more
exaly
Nihon rinsho. Japanese journal of clinical medicine, 1992
Na/H antiporter located in the plasma membrane is mandatory to maintain cell pH. Two isoforms with different sensitivities to amiloride have been identified. They seem to be products from different mRNAs. The amiloride-sensitive form exists in the non-epithelial cells and the basal membrane of the epithelial cells.
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Na/H antiporter located in the plasma membrane is mandatory to maintain cell pH. Two isoforms with different sensitivities to amiloride have been identified. They seem to be products from different mRNAs. The amiloride-sensitive form exists in the non-epithelial cells and the basal membrane of the epithelial cells.
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