نتایج جستجو برای: na h antiporter

تعداد نتایج: 785818  

2012
Faïçal Brini Khaled Masmoudi

Adaptation of plants to salt stress requires cellular ion homeostasis involving net intracellular Na(+) and Cl(-) uptake and subsequent vacuolar compartmentalization without toxic ion accumulation in the cytosol. Sodium ions can enter the cell through several low- and high-affinity K(+) carriers. Some members of the HKT family function as sodium transporter and contribute to Na(+) removal from ...

Journal: :Journal of molecular microbiology and biotechnology 2009
Judith Dzioba-Winogrodzki Olga Winogrodzki Terry A Krulwich Markus A Boin Claudia C Häse Pavel Dibrov

The mrp operon from Vibrio cholerae encoding a putative multisubunit Na(+)/H(+) antiporter was cloned and functionally expressed in the antiporter-deficient strain of Escherichia coli EP432. Cells of EP432 expressing Vc-Mrp exhibited resistance to Na(+) and Li(+) as well as to natural bile salts such as sodium cholate and taurocholate. When assayed in everted membrane vesicles of the E. coli EP...

Journal: :Journal of bacteriology 1998
R Ros C Montesinos A Rimon E Padan R Serrano

The bacterial Na+ (Li+)/H+ antiporter NhaA has been expressed in the yeast Saccharomyces cerevisiae. NhaA was present in both the plasma membrane and internal membranes, and it conferred lithium but not sodium tolerance. In cells containing the yeast Ena1-4 (Na+, Li+) extrusion ATPase, the extra lithium tolerance conferred by NhaA was dependent on a functional vacuolar H+ ATPase and correlated ...

Journal: :The Journal of biological chemistry 1982
T A Krulwich A A Guffanti R F Bornstein J Hoffstein

Activity of a Na+/H+ antiporter has been suggested to be critically involved in pH homeostasis in obligately alkalophilic bacteria (Krulwich, K. A., Mandel, K. G., Bornstein, R. F., and Guffanti, A. A. (1979) Biochem. Biophys. Res. Commun. 91, 58-62) and in Escherichia coli (Zilberstein, D., Padan, E., and Schuldiner, S. (1980) FEBS Lett. 116, 177-180). A concern with respect to these proposals...

1997
Nicolas Demaurex Robert R. Romanek John Orlowski Sergio Grinstein

We studied the ATP dependence of NHE-1, the ubiquitous isoform of the Na 1 /H 1 antiporter, using the whole-cell configuration of the patch-clamp technique to apply nucleotides intracellularly while measuring cytosolic pH (pH i ) by microfluorimetry. Na 1 /H 1 exchange activity was measured as the Na 1 -driven pH i recovery from an acid load, which was imposed via the patch pipette. In Chinese ...

Journal: :The Journal of clinical investigation 1990
M Baum

The present in vitro microperfusion study examined apical membrane Na+/H+ antiporter and basolateral membrane Na(HCO3)3 symporter activity in newborn and adult juxtamedullary proximal convoluted tubules. Proton fluxes were determined from the initial rate of change of intracellular pH after a change in the luminal or bathing solution, buffer capacity, and tubular volume of newborn and adult tub...

Journal: :The Journal of biological chemistry 1987
R T Miller A S Pollock

Sodium-proton antiporter activity can be modulated through changes Vmax and/or intracellular proton sensitivity of the antiporter. To characterize a parathyroid hormone (PTH)-induced decrease in antiporter activity in a continuous renal cell line (opossum kidney cells), the extracellular sodium and intracellular proton dependence of amiloride-inhibitable 22Na uptake was studied. The Km for extr...

Journal: :The Journal of biological chemistry 2005
Olga Kinclova-Zimmermannova Martin Zavrel Hana Sychrova

Yeast plasma membrane Na+/H+ antiporters are divided according to their substrate specificity in two distinct subfamilies. To identify amino acid residues responsible for substrate specificity determination (recognition of K+), the Zygosaccharomyces rouxii Sod2-22 antiporter (non-transporting K+) was mutagenized and a collection of ZrSod2-22 mutants that improved the KCl tolerance of a salt-sen...

Journal: :The Journal of biological chemistry 2000
M Venturi A Rimon Y Gerchman C Hunte E Padan H Michel

One of the most interesting properties of the NhaA Na(+)/H(+) antiporter of Escherichia coli is the strong regulation of its activity by pH. This regulation is accompanied by a conformational change that can be probed by digestion with trypsin and involves the hydrophilic loop connecting the transmembrane helices VIII-IX. In the present work we show that a monoclonal antibody (mAb), 1F6, recogn...

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