Abstract
Fatty acid-binding protein from bovine liver but not from bovine heart binds hematin in a saturable manner with high affinity. This property is not confined to a particular isoform as both, pI 6.0- and pI 7.0 L-FABP, bind hematin similarly. In competition experiments hematin and oleic acid could replace each other demonstrating that they share at least parts of the same binding site. Common structural features, i.e. the presence of carboxylic groups and of hydrophobic carbon chains led to the hypothesis that both ligands interact similarly with L-FABP. This was supported by the decrease of binding affinity for either ligand upon modification with phenylglyoxal. Modification in the presence of fatty acid revealed the protection of one of the two arginines of L-FABP. By peptide mapping and Edman degradation Arg122 was identified as the counterpart of the fatty acids carboxylic group.
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© 1993 Springer Science+Business Media Dordrecht
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Börchers, T., Spener, F. (1993). Involvement of arginine in the binding of heme and fatty acids to fatty acid-binding protein from bovine liver. In: Glatz, J.F.C., van der Vusse, G.J. (eds) Cellular Fatty Acid-Binding Proteins II. Developments in Molecular and Cellular Biochemistry, vol 10. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3096-1_4
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DOI: https://doi.org/10.1007/978-1-4615-3096-1_4
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