| Project/Area Number |
60570125
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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 |
Pathological medical chemistry
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| Research Institution | Division of Biochemistry, Institute of Basic Medical Sciences, University of tsukuba, Ibaraki,305. |
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Principal Investigator |
IYANAGI TAKASHI (1986) Institute of Basic Medical Sciences, University of Tsukuba, 基礎医学系, 助教授 (50001699)
井柳 堯 (1986) 筑波大学, 基礎医学系, 助教授
阿南 功一 (1985) 筑波大学, 基礎医学系, 教授
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| Co-Investigator(Kenkyū-buntansha) |
ANAN Koichi University of Tsukuba, 学長 (30013783)
FUJII-KURIYAMA Yoshiaki Cancer Institute, Japanease Foundation for Cancer Research, 研究所(生化学部), 部長 (00098146)
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| Project Period (FY) |
1985 – 1986
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| Project Status |
Completed (Fiscal Year 1986)
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| Budget Amount *help |
¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 1986: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1985: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | glucronosyltransferase / CDNA / membrane protein / induction by carcinogen / tissue specific expression / 誘導機構 / 臓器特異的発現 / アイソザイム |
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| Research Abstract |
The specific aim of this proposed project is to investigate structure analysis of isoenzymes of rat liver microsomal UDP-glucronosyltransferase (UDP-GT), which catalyzes glucronidation of bilirubin and steriods as well as xenobiotic compounds including carcinogens. Recent work on the cDNA cloning of UDPGT has established the existence of isoenzyme, but the relationship between individual isoenzymes and their corresponding cDNA is not substantiated, as detailed structure analysis of the purified protein has yet to be obtained. The project goals include: (1) the purification and characterization of 4-nitrophenol UDPGT, (2) the determination of partial amino acid sequences, including NH2-terminal and COOH-terminal, (3) the isolation and sequence analysis of its cDNA, (4) its amino acid sequence, (5) the induction of 4-nitrophenol UDP-GT by the treatment of 3-methylcholanthrene. This research will provide many clues concerning structure-function relationships of UDPGT isoenzymes.
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