Involvement of arginine in the binding of heme and fatty acids to fatty acid-binding protein from bovine liver.
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.
Börchers
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Department of Biochemistry, University of Münster, Germany.
Spener
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D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D002417:Cattle; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids / Q000378:metabolism*; D006418:Heme / Q000378:metabolism*; D006427:Hemin / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins; D010449:Peptide Mapping
D002352:Carrier Proteins; C493320:Fabp1 protein, mouse; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids; D009363:Neoplasm Proteins; D006418:Heme; D006427:Hemin; D001120:Arginine