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Fatty acid binding proteins from developing human fetal brain: Characterization and binding properties

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Abstract

Two fatty acid binding proteins (FABPs) of identicalM r, 13 kDa, have been isolated from developing human fetal brain. A delipidated 105,000 g supernatant was incubated with [1 -14C]oleate and subjected to a Sephacryl S-200 column followed by gel filtration chromatography on a Sephadex G-75 column and ion-exchange chromatography using a DEAE-Sephacel column. Purity was checked by UV spectroscopy, SDS-PAGE, isoelectric focusing and immunological cross-reactivity. The two FABPs designated as DE-I (pI 5.4) and DE-II (pI 6.9) showed cross-reactivity with each other and no alteration at the antigenic site during intrauterine development. Anti-human fetal brain FABP does not cross-react with purified human fetal heart, gut, lung or liver FABPs. The molecular mass of DE-I and DE-II is lower than those of fetal lung and liver FABPs. Like liver FABP, these proteins bind organic anions, fatty acids and acyl CoAs but differ in their binding affinities. Both DE-I and DE-II have been found to exhibit higher affinity for oleate (K d = 0.23 μM) than palmitate (K d = 0.9μM) or palmitoyl-CoA (K d = 0.96 μM), with DE-I binding less fatty acids than DE-II. DE-II is more efficient in transferring fatty acid from phospholipid vesjcles than DE-I indicating that human fetal brain FABPs may play a significant role in fatty acid transport in developing fetal brain.

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  1. Department of Biochemistry, University College of Science, University of Calcutta, 35, Ballygunge Circular Road, 700 019, Calcutta, India

    Durba Mukhopadhyay, Prabar K. Ghosh, Aparna Sen & Manju Mukherjea

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  1. Durba Mukhopadhyay
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  2. Prabar K. Ghosh
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  3. Aparna Sen
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  4. Manju Mukherjea
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Mukhopadhyay, D., Ghosh, P.K., Sen, A. et al. Fatty acid binding proteins from developing human fetal brain: Characterization and binding properties. J. Biosci. 23, 605–612 (1998). https://doi.org/10.1007/BF02709172

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  • DOI: https://doi.org/10.1007/BF02709172

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