| pubmed-article:17007 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17007 | lifeskim:mentions | umls-concept:C1704242 | lld:lifeskim |
| pubmed-article:17007 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:17007 | lifeskim:mentions | umls-concept:C1159651 | lld:lifeskim |
| pubmed-article:17007 | pubmed:issue | 3-4 | lld:pubmed |
| pubmed-article:17007 | pubmed:dateCreated | 1977-7-29 | lld:pubmed |
| pubmed-article:17007 | pubmed:abstractText | A vesicular microsomal fraction isolated from hog fundic mucosa demonstrates the capacity to take up equal amounts of RB+ and Cl-. The amount of the Rb+ uptake is sensitive to the extravesicular osmolarity, and rate of uptake is sensitive to temperature. 86Rb+ efflux is dependent upon the cation composition of the diluting solution. ATP, but not beta-gamma methylene ATP, induces a reversible efflux of 86Rb+ from loaded vesicles, and this is dependent upon a functional K+-ATPase. The ATP induced efflux is not affected by CCCP (carbonyl cyanide m-chlorophenylhydrazone) or TCS (tetrachlorosalicylanilide) nor by lipid soluble ions or valinomycin. Nigericin inhibits the efflux by 40%. Uptake of the lipid soluble ion 14C-SCN- has been demonstrated and is enhanced by ATP only in the presence of valinomycin. The results are consistent with a neutral or isopotential exchange of H+ for Rb+ mediated by K+-ATPase. | lld:pubmed |
| pubmed-article:17007 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17007 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17007 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17007 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17007 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:17007 | pubmed:issn | 0022-2631 | lld:pubmed |
| pubmed-article:17007 | pubmed:author | pubmed-author:SchwartzAA | lld:pubmed |
| pubmed-article:17007 | pubmed:author | pubmed-author:SachsGG | lld:pubmed |
| pubmed-article:17007 | pubmed:author | pubmed-author:SaccomaniGG | lld:pubmed |
| pubmed-article:17007 | pubmed:author | pubmed-author:SchackmannRR | lld:pubmed |
| pubmed-article:17007 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17007 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:17007 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:17007 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17007 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17007 | pubmed:pagination | 361-81 | lld:pubmed |
| pubmed-article:17007 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:17007 | pubmed:meshHeading | pubmed-meshheading:17007-En... | lld:pubmed |
| pubmed-article:17007 | pubmed:year | 1977 | lld:pubmed |
| pubmed-article:17007 | pubmed:articleTitle | Cation transport by gastric H+:K+ ATPase. | lld:pubmed |
| pubmed-article:17007 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17007 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:17007 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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