Abstract
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.
Highlights
In heart was provided by Fournier et al [16],who isolated and partially characterized a low M, fatty acid-binding protein
13401), it was shownthatbothratheartand liver protein. They reported that both palmitic acid fatty acid-binding proteins bind m2 ol of oleic acid or and oleic acid bind to ratliver Fatty acid-binding proteins (FABPs), but thatonly oleic acid palmitic acid/mol of protein
The structural and func- is bound by the rat heart fatty acid-binding protein [20]
Summary
Are members of a family of proteins derived from a common A description of the isolation, spectral properties, isoelectric ancestral gene [8, 9]. Attemptsto identify FABP in heart tissueused fatty heart FABPis presented inthe Miniprint Supplement under acid-binding assays to demonstrate that soluble protein frac- “Results.”. Tions from heart homogenates contain a low M , fatty acid- The amino acid compositions of rat heart and rat liver binding protein [1,12,13]. Indirect evidence for the existence FABP determined in thepresent work are compared in Table of a form of FABP in heart tissue was provided by Ockner I to the amino acid compositions (from cDNA sequences) of a d Manning [5] using an antibody directed against jejeunal FABP from rat liver, rat intestine, and 3T3 adipocytes. Full size photocopies are included in the microfilm edition of the Journal that is available from Waverly Press. Amino acid composition of FABP fromrat heart, liver and intestine, and 3T3 adipocytes. The values in parentheses refer to the number of amino acid residues based on the nucleotide sequence
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