| Project/Area Number |
01570145
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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 |
General medical chemistry
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| Research Institution | Osaka Bioscience Instutute |
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Principal Investigator |
WATANABE Kikuko Osaka Bioscience Institute, 2nd Dept., Researcher, 第2研究部, 研究員 (90211672)
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| Co-Investigator(Kenkyū-buntansha) |
陳 蘭英 (財)大阪バイオサイエンス研究所, 第2研究部, STAフェロー
KUCHINKE Wol (財)大阪バイオサイエンス研究所, 第2研究部, STAフェロー
HAYAISHI Osamu Osaka Bioscience Institute, Director, 所長 (40025507)
CHEN Lan-Ying Osaka Bioscience Institute, 2nd Dept., STA Fellow
KUCHINKE Welfgang Osaka Bioscience Institute, 2nd Dept., STA Fellow
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| Project Period (FY) |
1989 – 1991
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| Project Status |
Completed (Fiscal Year 1991)
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| Budget Amount *help |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1991: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1990: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1989: ¥800,000 (Direct Cost: ¥800,000)
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| Keywords | Prostaglandins / PGF Synthase / 9alpha, 11beta -PGF_2 / Isozyme / PGF2alpha / PGF_2α / 光親和ラベル / PGD還元活性 / 多機能酵素 / 活性部位 / 構造 / 9α・11βーPGF_2 / アルド・ケト還元酵素 / クリスタリン |
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| Research Abstract |
1. prostaglandin(PG)F synthase from bovine lung is a monomeric protein with a Mr of 36, 666 consisting of 323 amino acid residues. The enzyme is a dual function enzyme catalyzing the reduction of PGH_2 to PGF_<>a and PGD_2 to 9a, 11b-PGF_2 at different active sites on the swne molecule. The enzyme is constructed from at least two domains, and ^<195>Pro is related to the function of the binding site of PGD_2.
2. About 50th, 200th, and 280th amino acid residues from N-terminus of PGF synthase are modified with the derivative of PGD_2, and so these amino acids may construct the active site for PGD_2.
3. We reported that new type of PGF synthase was discovered in bovine liver which shows cross-reactivity with anti-PGF synthase antibody, but that the enzymatic property of liver PGF synthase was different from that of lung PGF synthase.
We isolated cDNA clone which has 3 amino acids exchanged in the primary structure of lung PGF synthase. The property of the expressed protein of this clone was almost the same as that of lung PGF synthase, and the enzyme was the different type of liver PGF synthase. PGF synthase has at least two types of isozyme, and has the different biological role of each isozyme.
Another structure-function study to be carried out involves prostaglandin(PG)F synthase. The enzyme is a dual function enzyme. The problem of structure-function relationship in this enzyme will be studied by variety of methods, including biochemical, molecular biological and protein chemical methods using X-ray analysis and NMR. Fourthermore, PGF synthase has at least two types of isozyme. The relationships of these isozymes will also be clarified by genomic study of PGF synthase.
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