| pubmed-article:1894608 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1894608 | lifeskim:mentions | umls-concept:C0021853 | lld:lifeskim |
| pubmed-article:1894608 | lifeskim:mentions | umls-concept:C0015684 | lld:lifeskim |
| pubmed-article:1894608 | lifeskim:mentions | umls-concept:C0032473 | lld:lifeskim |
| pubmed-article:1894608 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:1894608 | lifeskim:mentions | umls-concept:C0163315 | lld:lifeskim |
| pubmed-article:1894608 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:1894608 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:1894608 | pubmed:dateCreated | 1991-10-21 | lld:pubmed |
| pubmed-article:1894608 | pubmed:abstractText | Binding and proximity relationships of fatty acids with recombinant rat liver fatty acid-binding protein (L-FABP) and intestinal fatty acid-binding protein (I-FABP) were studied with absorption and fluorescence spectroscopy. Protein aromatic amino acids were examined in the absence and presence of bound fatty acid. Second derivative absorbance spectroscopy of the apo- and holoproteins suggested that fatty acid binding altered the conformation of L-FABP, but not of I-FABP. Fatty acid binding also blocked the accessibility of L-FABP tyrosine and I-FABP tryptophan to Stern-Volmer quenching by acrylamide, indicating that these amino acids were present in the fatty acid-binding pocket. Forster energy transfer from I-FABP tryptophan to bound cis-parinaric acid resulted in quenching of tryptophan lifetime and appearance of sensitized lifetime of bound cis-parinaric acid. The calculated donor-acceptor distances were 16.9 +/- 0.6 and 19.2 +/- 0.3 A for I-FABP and L-FABP, respectively. Absorbance spectral shifts and ratios of fluorescence excitation maxima indicated that the parinaric acid microenvironment in the fatty acid-binding site of I-FABP was much less polar than that of L-FABP. Parinaric acids displayed similar rotational correlation time and limiting anisotropy when bound to I-FABP and to L-FABP. These results are consistent with a close proximity of bound fatty acids to the tyrosine and tryptophan residues and with immobilization of the polyene fatty acids in the fatty acid-binding site(s) of L-FABP and I-FABP. The two proteins differ in that only L-FABP has two fatty acid-binding sites and appears to undergo significant conformational change upon fatty acid binding. | lld:pubmed |
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| pubmed-article:1894608 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1894608 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1894608 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1894608 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:1894608 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1894608 | pubmed:author | pubmed-author:SchroederFF | lld:pubmed |
| pubmed-article:1894608 | pubmed:author | pubmed-author:JeffersonJ... | lld:pubmed |
| pubmed-article:1894608 | pubmed:author | pubmed-author:NemeczGG | lld:pubmed |
| pubmed-article:1894608 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1894608 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1894608 | pubmed:volume | 266 | lld:pubmed |
| pubmed-article:1894608 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1894608 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1894608 | pubmed:pagination | 17112-23 | lld:pubmed |
| pubmed-article:1894608 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:1894608 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1894608 | pubmed:articleTitle | Polyene fatty acid interactions with recombinant intestinal and liver fatty acid-binding proteins. Spectroscopic studies. | lld:pubmed |
| pubmed-article:1894608 | pubmed:affiliation | Department of Pharmacology and Cell Biophysics, University of Cincinnati Medical Center, Ohio 45267-0004. | lld:pubmed |
| pubmed-article:1894608 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1894608 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1894608 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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