pubmed-article:1970294 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1970294 | lifeskim:mentions | umls-concept:C0004654 | lld:lifeskim |
pubmed-article:1970294 | lifeskim:mentions | umls-concept:C0039065 | lld:lifeskim |
pubmed-article:1970294 | lifeskim:mentions | umls-concept:C0013126 | lld:lifeskim |
pubmed-article:1970294 | lifeskim:mentions | umls-concept:C0061467 | lld:lifeskim |
pubmed-article:1970294 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:1970294 | pubmed:dateCreated | 1990-5-31 | lld:pubmed |
pubmed-article:1970294 | pubmed:abstractText | Active accumulation of neurotransmitters by synaptic vesicles is an essential component of the synaptic transmission cycle. Isolated vesicles show energy-dependent uptake of several transmitters by processes which are apparently mediated by a proton electrochemical potential across the vesicle membrane. Although this energy gradient is probably generated by a proton ATPase, the functional separation of ATP cleavage and transmitter uptake activity has only been shown clearly for monoamine transport. We report here that the light-driven proton pump, bacteriorhodopsin, can replace the endogenous proton ATPase in proteoliposomes reconstituted from vesicular detergent extracts. The system shows light-dependent uptake of glutamate with properties very similar to those observed in intact vesicles, e.g. chloride dependence or stimulation by NH4+. Our experiments show that the proton pump and the glutamate transporter are separate entities and provide a powerful tool for further characterization of the glutamate carrier. | lld:pubmed |
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pubmed-article:1970294 | pubmed:language | eng | lld:pubmed |
pubmed-article:1970294 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1970294 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1970294 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1970294 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1970294 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1970294 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1970294 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:1970294 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1970294 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1970294 | pubmed:month | May | lld:pubmed |
pubmed-article:1970294 | pubmed:issn | 0261-4189 | lld:pubmed |
pubmed-article:1970294 | pubmed:author | pubmed-author:JahnRR | lld:pubmed |
pubmed-article:1970294 | pubmed:author | pubmed-author:MaycoxP RPR | lld:pubmed |
pubmed-article:1970294 | pubmed:author | pubmed-author:DeckwerthTT | lld:pubmed |
pubmed-article:1970294 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1970294 | pubmed:volume | 9 | lld:pubmed |
pubmed-article:1970294 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1970294 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1970294 | pubmed:pagination | 1465-9 | lld:pubmed |
pubmed-article:1970294 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:1970294 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:1970294 | pubmed:articleTitle | Bacteriorhodopsin drives the glutamate transporter of synaptic vesicles after co-reconstitution. | lld:pubmed |
pubmed-article:1970294 | pubmed:affiliation | Department of Neurochemistry, Max-Planck-Institute for Psychiatry, Martinsried, FRG. | lld:pubmed |
pubmed-article:1970294 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1970294 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:1970294 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |