| pubmed-article:17189259 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17189259 | lifeskim:mentions | umls-concept:C0666163 | lld:lifeskim |
| pubmed-article:17189259 | lifeskim:mentions | umls-concept:C1621938 | lld:lifeskim |
| pubmed-article:17189259 | lifeskim:mentions | umls-concept:C0456962 | lld:lifeskim |
| pubmed-article:17189259 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:17189259 | pubmed:dateCreated | 2007-2-19 | lld:pubmed |
| pubmed-article:17189259 | pubmed:abstractText | The transport of ammonia/ammonium is fundamental to nitrogen metabolism in all forms of life. So far, no clear picture has emerged as to whether a protein channel is capable of transporting exclusively neutral NH(3) while excluding H(+) and NH(4)(+). Our research is the first stoichiometric study to show the selective transport of NH(3) by a membrane channel. The purified water channel protein aquaporin-8 was reconstituted into planar bilayers, and the exclusion of NH(4)(+) or H(+) was established by ensuring a lack of current under voltage clamp conditions. The single channel water permeability coefficient of 1.2 x 10(-14) cm(3)/subunit/s was established by imposing an osmotic gradient across reconstituted planar bilayers, and resulting minute changes in ionic concentration close to the membrane surface were detected. It is more than 2-fold smaller than the single channel ammonia permeability (2.7 x 10(-14) cm(3)/subunit/s) that was derived by establishing a transmembrane ammonium concentration gradient and measuring the resulting concentration increases adjacent to the membrane. This permeability ratio suggests that electrically silent ammonia transport may be the main function of AQP8. | lld:pubmed |
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| pubmed-article:17189259 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17189259 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17189259 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17189259 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17189259 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:17189259 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:17189259 | pubmed:author | pubmed-author:AhnT ITI | lld:pubmed |
| pubmed-article:17189259 | pubmed:author | pubmed-author:KooM JMJ | lld:pubmed |
| pubmed-article:17189259 | pubmed:author | pubmed-author:AgrePeterP | lld:pubmed |
| pubmed-article:17189259 | pubmed:author | pubmed-author:PohlPeterP | lld:pubmed |
| pubmed-article:17189259 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17189259 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:17189259 | pubmed:volume | 282 | lld:pubmed |
| pubmed-article:17189259 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17189259 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17189259 | pubmed:pagination | 5296-301 | lld:pubmed |
| pubmed-article:17189259 | pubmed:dateRevised | 2011-7-26 | lld:pubmed |
| pubmed-article:17189259 | pubmed:meshHeading | pubmed-meshheading:17189259... | lld:pubmed |
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| pubmed-article:17189259 | pubmed:meshHeading | pubmed-meshheading:17189259... | lld:pubmed |
| pubmed-article:17189259 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17189259 | pubmed:articleTitle | Fast and selective ammonia transport by aquaporin-8. | lld:pubmed |
| pubmed-article:17189259 | pubmed:affiliation | Institut für Biophysik, Kepler Universität Linz, Altenbergerstrasse 69, A-4040 Linz, Austria. | lld:pubmed |
| pubmed-article:17189259 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17189259 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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