RGD Reference Report - Characterization of a fatty acid-binding protein from rat heart. - Rat Genome Database

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Characterization of a fatty acid-binding protein from rat heart.

Authors: Offner, GD  Troxler, RF  Brecher, P 
Citation: Offner GD, etal., J Biol Chem. 1986 Apr 25;261(12):5584-9.
RGD ID: 1582414
Pubmed: PMID:3957934   (View Abstract at PubMed)

A fatty acid-binding protein has been isolated from rat heart and purified by gel filtration chromatography on Sephadex G-75 and anion-exchange chromatography on DE52. The circular dichroic spectrum of this protein was not affected by protein concentration, suggesting that it does not aggregate into multimers. Computer analyses of the circular dichroic spectrum predicted that rat heart fatty acid-binding protein contains approximately 22% alpha-helix, 45% beta-form and 33% unordered structure. Immunological studies showed that the fatty acid-binding proteins from rat heart and rat liver are immunochemically unrelated. The amino acid composition and partial amino acid sequence of the heart protein indicated that it is structurally related to, but distinct from, other fatty acid-binding proteins from liver, intestine, and 3T3 adipocytes. Using a binding assay which measures the transfer of fatty acids between donor liposomes and protein (Brecher, P., Saouaf, R., Sugarman, J. M., Eisenberg, D., and LaRosa, K. (1984) J. Biol. Chem. 259, 13395-13401), it was shown that both rat heart and liver fatty acid-binding proteins bind 2 mol of oleic acid or palmitic acid/mol of protein. The structural and functional relationship of rat heart fatty acid-binding protein to fatty acid-binding proteins from other tissues is discussed.

Objects referenced in this article
Gene Fabp3 fatty acid binding protein 3 Rattus norvegicus

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