| pubmed-article:2108440 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2108440 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:2108440 | lifeskim:mentions | umls-concept:C1622418 | lld:lifeskim |
| pubmed-article:2108440 | lifeskim:mentions | umls-concept:C1882598 | lld:lifeskim |
| pubmed-article:2108440 | lifeskim:mentions | umls-concept:C1420206 | lld:lifeskim |
| pubmed-article:2108440 | lifeskim:mentions | umls-concept:C1521827 | lld:lifeskim |
| pubmed-article:2108440 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:2108440 | pubmed:dateCreated | 1990-5-4 | lld:pubmed |
| pubmed-article:2108440 | pubmed:abstractText | Electrogenic sodium- and chloride-dependent gamma-aminobutyric acid (GABA) transport in crude synaptosomal membrane vesicles is partly inhibited by saturating levels of either of the substrate analogues cis-3-aminocyclohexanecarboxylic acid (ACHC) or beta-alanine. However, both of them together potently and fully inhibit the process. Transport of beta-alanine, which exhibits an apparent Km of about 44 microM, is also electrogenic and sodium and chloride dependent and competitively inhibited by GABA with a Ki of about 3 microM. This value is very similar to the Km of 2-4 microM found for GABA transport. On the other hand, ACHC does not inhibit beta-alanine transport at all. Upon solubilization of the membrane proteins with cholate and fractionation with ammonium sulfate, a fraction is obtained which upon reconstitution into proteoliposomes exhibits 4- to 10-fold-increased GABA transport. This activity is fully inhibited by low concentrations of ACHC and is not sensitive at all to beta-alanine. GABA transport in this preparation exhibits an apparent Km of about 2.5 microM and it is competitively inhibited by ACHC (Ki approximately 7 microM). These data indicate the presence of two GABA transporter subtypes in the membrane vesicles: the A type, sensitive to ACHC, and the B type, sensitive to beta-alanine. | lld:pubmed |
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| pubmed-article:2108440 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2108440 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2108440 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2108440 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:2108440 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2108440 | pubmed:author | pubmed-author:KannerB IBI | lld:pubmed |
| pubmed-article:2108440 | pubmed:author | pubmed-author:BendahanAA | lld:pubmed |
| pubmed-article:2108440 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2108440 | pubmed:volume | 87 | lld:pubmed |
| pubmed-article:2108440 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2108440 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2108440 | pubmed:pagination | 2550-4 | lld:pubmed |
| pubmed-article:2108440 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2108440 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2108440 | pubmed:articleTitle | Two pharmacologically distinct sodium- and chloride-coupled high-affinity gamma-aminobutyric acid transporters are present in plasma membrane vesicles and reconstituted preparations from rat brain. | lld:pubmed |
| pubmed-article:2108440 | pubmed:affiliation | Department of Biochemistry, Hadassah Medical School, Hebrew University, Jerusalem, Israel. | lld:pubmed |
| pubmed-article:2108440 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2108440 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2108440 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:2108440 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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