Chemical Structure and Physiological Function of Hydrophobic Molecule-binding Protein in Cytosols

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Hydrophobic molecule-binding proteins in cytosols were investigated for their structure and function relationship and for cellular distribution.1. A novel molecular species of rat liver fatty acid binding protein having isoaspartyl residue at position 105 was identified and its physiological significance was investigated.2. Photo-sensitive affinity labels were synthesized and used for identification of hydrophobic ligand-binding site(s) in fatty acid binding protein. Oleoylimidazolide was also synthesized and shown to be an effective affinity-label for fatty acid binding region.3. A hydrophobic carcinogenic dye, amino-azobenzene, was administered to rats and binding site for its metabolically activated product was identified. Two other binding proteins were also identified.4. A new hydrophobic molecule-binding protein was isolated from intestinal epithelium and fully sequenced.5. Two fatty acid binding proteins were isolated from rat kidneys. It was shown that one of them is a member of lipocalin superfamily and the other heart type fatty acid binding protein.