| Project/Area Number |
20580221
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Fisheries chemistry
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| Research Institution | Kyushu University |
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Principal Investigator |
YUJI Oshima Kyushu University, 農学研究院, 教授 (70176874)
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| Project Period (FY) |
2007 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2010: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2009: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2008: ¥2,990,000 (Direct Cost: ¥2,300,000、Indirect Cost: ¥690,000)
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| Keywords | 静菌 / 生体防御 / 低分子結合性 / リポカリン / 静菌活性 / ヒラメ / 遺伝子組換え体 / 遺伝子組替え / シデロフォア |
|---|
| Research Abstract |
Tributyltin (TBT) is well-known as a strong endocrine disruptor and has been detected at high concentrations in the blood of fishes living in coastal areas. In our previous studies, we identified TBT-binding proteins (TBT-bp1 and 2) bound to TBT in the blood of Japanese flounder (Paralichthys olivaceus) and determined that TBT-bps were have a function that would bind to TBT and then be excreted into the mucus. TBT-bps are a member of the lipocalin family of proteins which bind to small hydrophobic molecules. In this study, we expressed a recombinant TBT-bp1and -bp2 (rTBT-bp1, 2) in a baculovirus expression system and purified the protein from the hemolymph of silkworm larvae injected with recombinant baculovirus. From the results of binding assay of rTBT-bp 2 to some chemicals, TBT-bp2 show affinity to TBT but not to lauric acid, palmitic acid and tearic acid. Furthermore, rTBT-bp1 may inhibit the growth of fish dieseas bacteria Edwardsiella tarda, suggesting bacteriostasis activity.
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