| Project/Area Number |
09680637
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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 |
Functional biochemistry
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| Research Institution | University of East Asia (1999-2000)
Osaka Bioscience Institute (1997-1998) |
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Principal Investigator |
WATANABE Kikuko University of East Asia, Department of Life Science and Technology, Professor, 工学部, 教授 (90211672)
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| Co-Investigator(Kenkyū-buntansha) |
OHISHI Kenji University of East Asia, Department of Life Science and Technology, Professor, 工学部, 教授 (10152042)
MATSUMURA Hitoshi Osaka Medical College, Department of Neuropsychiatry, Assistant Professor., 精神神経科, 講師 (50173886)
ITO Seiji Kansai Medical University, Department of Medical Chemistory, Professor, 医化学教室, 教授 (80201325)
早石 修 (財)大阪バイオサイエンス研究所, 第2研究部, 名誉所長 (40025507)
鈴木 登志子 徳島大学, 第一解剖学教室, 助手
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| Project Period (FY) |
1997 – 2000
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| Project Status |
Completed (Fiscal Year 2000)
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| Budget Amount *help |
¥3,200,000 (Direct Cost: ¥3,200,000)
Fiscal Year 2000: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1999: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1998: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1997: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | Prostaglandin / Membrane-bound enzyme / PGE synthase / Purification of Enzyme / Cloning / 酵素 / 精製 / 膜結合 / グルタチオン |
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| Research Abstract |
E series of prostaglandin (PG)s were first discovered in sheep seminal vesicles. PGE_2 is widely distributed in various organs, and exhibits various biological activities such as smooth muscle dilatation/contraction, Na^+ excretion, body temperature regulation, inhibition of gastric acid secretion, and inhibition of immune responses. PGE synthase (EC.5. 3. 99. 3.) catalyzes the conversion of PGH_2 to PGE_2. In 1997, we reported that PGE synthase activity is widely distributed in the microsomal fractions of rat organs. Most of the PGE synthase activities in these organs absolutely required glutathione (GSH). In contrast, the enzyme activity in the heart, spleen, and uterine microsomes required SH-reducing reagents including dithiothreitol (DTT), GSH, or β- mercaptoethanol (β-Mer), but the requirement for its catalytic activity was not specific for GSH.We purified the GSH specific PGE synthase from bovine heart microsomes to apparent homogeneity, and partially purified the GSH unspecific PGE synthase from sheep seminal vesicle microsomes. We examined their molecular and catalytic properties.
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