Characterization and binding properties of fatty acid-binding proteins from human, pig, and rat heart.

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Paulussen RJ, van der Logt CP, Veerkamp JH

Characterization and binding properties of fatty acid-binding proteins from human, pig, and rat heart.

Arch Biochem Biophys. 1988 Aug 1;264(2):533-45. doi: 10.1016/0003-9861(88)90319-0.

PubMed ID

3401011 [ View in PubMed

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Abstract

Fatty acid-binding proteins (FABPs) were isolated from the cytosols of hearts of man, pig, and rat by gel filtration and anion-exchange chromatography. The heart FABPs had a Mr of about 15,000 (pig, rat) and 15,500 (man); pI values were 5.2, 4.9, and 5.0 for human, pig, and rat heart, respectively. In contrast to liver FABPs, tryptophan was present in the heart FABPs. Binding characteristics for long-chain fatty acids determined with the radiochemical Lipidex assay were comparable for all three proteins. Heart FABPs also bind palmitoyl-CoA and -carnitine with an affinity comparable to that for palmitic acid. Other ligands investigated, heme, bilirubin, cholesterol, retinoids, and prostaglandins, could not compete with oleic acid for binding by human heart FABP. Binding parameters of FABP for oleic acid from multilamellar liposomes were comparable to those from the Lipidex binding assay. Immunological interspecies cross-reactivity with antisera against the heart FABPs was much higher between man and pig than between rat and man or pig. None of the antisera reacted with liver FABPs. The IgG fraction of anti-human heart FABP serum inhibited fatty acid binding to human heart FABP.

DrugBank Data that Cites this Article

Drug Carriers

Drug	Carrier	Kind	Organism	Pharmacological Action	Actions
Oleic Acid	Fatty acid-binding protein, heart	Protein	Humans	Unknown	Not Available	Details