| pubmed-article:4360536 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:4360536 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:4360536 | lifeskim:mentions | umls-concept:C1622418 | lld:lifeskim |
| pubmed-article:4360536 | lifeskim:mentions | umls-concept:C0001962 | lld:lifeskim |
| pubmed-article:4360536 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
| pubmed-article:4360536 | lifeskim:mentions | umls-concept:C1159492 | lld:lifeskim |
| pubmed-article:4360536 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
| pubmed-article:4360536 | lifeskim:mentions | umls-concept:C0349590 | lld:lifeskim |
| pubmed-article:4360536 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:4360536 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:4360536 | pubmed:dateCreated | 1974-4-18 | lld:pubmed |
| pubmed-article:4360536 | pubmed:abstractText | Ethanol stimulated the uptake of l-alanine into isolated membrane vesicles of a marine pseudomonad at a rate and to an extent comparable with that obtained with reduced nicotinamide adenine dinucleotide (NADH) or the artificial electron donor ascorbate-N, N, N', N'-tetramethyl-p-phenylenediamine (ascorbate-TMPD). Methanol and branched-chain alcohols had little or no capacity to energize transport. No quantitative relationship was found between the ability of a compound to induce oxygen uptake and to energize transport, since with ethanol initial rates of oxygen uptake were approximately 4% of that obtained with NADH or ascorbate-TMPD. Cytochrome analysis revealed that NADH and ethanol reduced cytochromes b and c, whereas ascorbate-TMPD coupled primarily at the level of cytochrome c. Approximately 25% of the cytochromes reduced by dithionite were reducible by ethanol. Ethanol reduction of both cytochromes b and c was prevented by 2-heptyl-4-hydroxyquinoline-N-oxide, p-chloromercuribenzoate, N-ethylmaleimide, and iodoacetate. The ethanol- and NADH-energized transport systems for l-alanine were subject to quantitatively similar inhibition by cyanide, 2-heptyl-4-hydroxyquinoline-N-oxide, 2, 4-dinitrophenol, and the sulfhydryl reagents p-chloromercuribenzoate, N-ethylmaleimide, and iodoacetate. In contrast, for ascorbate-TMPD-driven transport, only cyanide and 2, 4-dinitrophenol remained fully effective as inhibitors, p-chloromercuribenzoate was only half as effective, and the other compounds stimulated transport. Inhibition of ethanol oxidation strikingly paralleled the inhibition of ethanol-driven transport for each of the inhibitors, including 2, 4-dinitrophenol. Marked differences between inhibition of oxygen uptake and inhibition of transport were observed when NADH or ascorbate-TMPD were the electron donors. The data indicate that only a small proportion of the respiratory chain complexes in the membrane vesicles are involved in transport and these are efficiently coupled to ethanol oxidation. The results also suggest that when 2, 4-dinitrophenol inhibits transport it is not acting as an uncoupling agent. | lld:pubmed |
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| pubmed-article:4360536 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:4360536 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:4360536 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:4360536 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:4360536 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:4360536 | pubmed:author | pubmed-author:SprottG DGD | lld:pubmed |
| pubmed-article:4360536 | pubmed:author | pubmed-author:MacLeodR ARA | lld:pubmed |
| pubmed-article:4360536 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:4360536 | pubmed:volume | 117 | lld:pubmed |
| pubmed-article:4360536 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:4360536 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:4360536 | pubmed:pagination | 1043-54 | lld:pubmed |
| pubmed-article:4360536 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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| pubmed-article:4360536 | pubmed:year | 1974 | lld:pubmed |
| pubmed-article:4360536 | pubmed:articleTitle | Nature of the specificity of alcohol coupling to L-alanine transport into isolated membrane vesicles of a marine pseudomonad. | lld:pubmed |
| pubmed-article:4360536 | pubmed:publicationType | Journal Article | lld:pubmed |
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