| pubmed-article:8089118 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8089118 | lifeskim:mentions | umls-concept:C0242915 | lld:lifeskim |
| pubmed-article:8089118 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8089118 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8089118 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:8089118 | lifeskim:mentions | umls-concept:C0033727 | lld:lifeskim |
| pubmed-article:8089118 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8089118 | lifeskim:mentions | umls-concept:C0457405 | lld:lifeskim |
| pubmed-article:8089118 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8089118 | pubmed:issue | 38 | lld:pubmed |
| pubmed-article:8089118 | pubmed:dateCreated | 1994-10-20 | lld:pubmed |
| pubmed-article:8089118 | pubmed:abstractText | We have previously demonstrated that the V0 domain of the coated vesicle V-ATPase, a 250-kDa integral complex, does not form a functional proton channel (Zhang, J., Myers, M., and Forgac, M. (1992) J. Biol. Chem. 267, 9773-9778). In the present study we describe dissociation of the V0 complex and separation of the V0 subunits by gel filtration. Dicyclohexylcarbodiimide-inhibitable passive proton conductance of reconstituted vesicles containing reassembled V0 subunits was measured in response to a K+/valinomycin-generated membrane potential. We observed that reconstituted vesicles containing the 17/19-kDa subunits carried out passive proton transport, with the addition of the 38- and 100-kDa subunits increasing proton conductance. Reconstituted vesicles containing the 38- and/or 100-kDa subunits showed no proton transport. Partial separation of the 17- and 19-kDa subunits revealed that the 17-kDa subunit alone carried out proton transport, with increased conductance on the addition of the 19-kDa subunit. These results indicate that the V0 domain possesses the information necessary to form a dicyclohexylcarbodiimide-inhibitable passive proton channel. Bafilomycin binding by native and reassembled V0 complexes was also measured by their ability to protect V-ATPase activity against bafilomycin inhibition. The native V0 domain, the isolated 100-kDa subunit and the 100/38-kDa subunits were able to protect against inhibition by bafilomycin, suggesting that the binding site for bafilomycin resides on the 100-kDa subunit. | lld:pubmed |
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| pubmed-article:8089118 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8089118 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8089118 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8089118 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8089118 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8089118 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8089118 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8089118 | pubmed:author | pubmed-author:FengYY | lld:pubmed |
| pubmed-article:8089118 | pubmed:author | pubmed-author:ZhangJJ | lld:pubmed |
| pubmed-article:8089118 | pubmed:author | pubmed-author:ForgacMM | lld:pubmed |
| pubmed-article:8089118 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8089118 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:8089118 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:8089118 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8089118 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8089118 | pubmed:pagination | 23518-23 | lld:pubmed |
| pubmed-article:8089118 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8089118 | pubmed:meshHeading | pubmed-meshheading:8089118-... | lld:pubmed |
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| pubmed-article:8089118 | pubmed:meshHeading | pubmed-meshheading:8089118-... | lld:pubmed |
| pubmed-article:8089118 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8089118 | pubmed:articleTitle | Proton conduction and bafilomycin binding by the V0 domain of the coated vesicle V-ATPase. | lld:pubmed |
| pubmed-article:8089118 | pubmed:affiliation | Department of Cellular and Molecular Physiology, Tufts University School of Medicine, Boston, Massachusetts 02111. | lld:pubmed |
| pubmed-article:8089118 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8089118 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:8089118 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8089118 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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