Plasma-membrane fatty-acid-binding protein in human placenta-identification and characterization

Fiona Margaret Campbell, S Taffesse, Margaret Jane Gordon, A K Duttaroy

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    Abstract

    A plasma membrane fatty-acid-binding protein (FABP(pm)) with a molecular mass of similar to 40kDa has been identified in human placenta. Binding of both [C-14] oleate and [C-14] linoleate to human placental membranes was found to be time and temperature dependent. Sulphobromophthalein and alpha-tocopherol did not show competition with the [C-14] fatty acid binding. These data suggest that the binding sites are specific for fatty acids. incubation of the membranes with trypsin reduced fatty acid binding activity, indicating that the binding sites were protein in nature. A FABP(pm) was then solubilzed from placental membranes and purified to electrophoretic homogeneity. The fatty acid binding activity of the purified protein was confirmed by autoradioblotting. Polyclonal antiserum raised to FABP(pm) reduced fatty acid binding to placental membrane significantly compared with preimmune serum. The pI value and the amino acid composition of the protein suggest that the placental FABP(pm) is different from the previously identified hepatic FABP(pm). (C) 1995 Academic Press, Inc.

    Original languageEnglish
    Pages (from-to)1011-1017
    Number of pages7
    JournalBiochemical and Biophysical Research Communications
    Volume209
    Issue number3
    DOIs
    Publication statusPublished - 26 Apr 1995

    Keywords

    • RAT-LIVER
    • PURIFICATION
    • rat-liver
    • purification

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