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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1988-6-14
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pubmed:abstractText |
In order to permit future characterization and possible isolation of the Na+-H+ exchanger from the apical membrane of proximal tubular cells, studies were performed to solubilize and reconstitute this transporter. Rabbit brush border membranes were prepared by a magnesium aggregation method, solubilized with the detergent octyl glucoside, and reconstituted into artificial phospholipid vesicles. In the presence of a pH gradient (pHin 6.0, pHout 8.0), the uptake of 1 mM 22Na+ into the proteoliposomes was five- to sevenfold higher than into liposomes. Amiloride (2 mM) inhibited proton gradient-stimulated uptake of sodium by 50%. As compared to proton gradient conditions, the uptake of sodium was lower in the absence of a pH gradient but was significantly higher when the outside and inside pH was 6.0 than 8.0. The Ka for sodium in reconstituted proteoliposomes studied under pH gradient conditions was 4 mM. The uptake of sodium in proteoliposomes prepared from heat-denatured membrane proteins was significantly decreased. These studies demonstrate that proteoliposomes prepared from octyl glucoside-solubilized brush border membrane proteins and asolectin exhibit proton gradient-stimulated, amiloride-inhibitable, electroneutral uptake of sodium. The ability to solubilize and reconstitute the Na+-H+ exchanger from the apical membrane of the proximal tubule will be of value in isolating and characterizing this transporter.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amiloride,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Liposomes,
http://linkedlifedata.com/resource/pubmed/chemical/Proteolipids,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Hydrogen Antiporter,
http://linkedlifedata.com/resource/pubmed/chemical/proteoliposomes
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pubmed:status |
MEDLINE
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pubmed:issn |
0022-2631
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
101
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2835484-Amiloride,
pubmed-meshheading:2835484-Animals,
pubmed-meshheading:2835484-Carrier Proteins,
pubmed-meshheading:2835484-Kidney,
pubmed-meshheading:2835484-Kinetics,
pubmed-meshheading:2835484-Liposomes,
pubmed-meshheading:2835484-Microvilli,
pubmed-meshheading:2835484-Proteolipids,
pubmed-meshheading:2835484-Rabbits,
pubmed-meshheading:2835484-Sodium,
pubmed-meshheading:2835484-Sodium-Hydrogen Antiporter,
pubmed-meshheading:2835484-Solubility
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pubmed:year |
1988
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pubmed:articleTitle |
Solubilization and reconstitution of renal brush border Na+-H+ exchanger.
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pubmed:affiliation |
Department of Internal Medicine, Pharmacology, and Physiology, University of Texas Medical School, Houston 77225.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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