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      https://www.ias.ac.in/article/fulltext/jbsc/023/05/0605-0612

    • Keywords

       

      Fatty acid binding protein; fetal brain; liposome

    • Abstract

       

      Two fatty acid binding proteins (FABPs) of identicalMr, 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 (Kd = 0.23 μM) than palmitate (Kd = 0.9μM) or palmitoyl-CoA (Kd = 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.

    • Author Affiliations

       

      Durba Mukhopadhyay1 Prabar K Ghosh1 Aparna Sen1 Manju Mukherjea1

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

       
  • Journal of Biosciences | News

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