1992 Fiscal Year Final Research Report Summary
Chemical Structure and Physiological Function of Hydrophobic Molecule-binding Protein in Cytosols
| Project/Area Number |
03680143
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
物質生物化学
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| Research Institution | Niigata University |
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Principal Investigator |
ODANI Shoji NIIGATA UNIVERSITY, FAC. SCI., Professor, 理学部, 教授 (60018702)
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| Project Period (FY) |
1991 – 1992
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| Keywords | fatty acid binding protein / affinity labeling / rat liver / protein chemistry / chemical carcinogen / azo-dye / amino acid sequence / kidney |
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| Research Abstract |
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.
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