| Project/Area Number |
61560100
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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 |
応用生物化学・栄養化学
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| Research Institution | Department of Nutrition, School of Medicine, The University of Tokushima |
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Principal Investigator |
OGAWA Tadashi Associate Professor, Department of Nutrition, School of Medicine, The University of Tokushima, 医学部, 助教授 (80027193)
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| Co-Investigator(Kenkyū-buntansha) |
KIMOTO Masumi Assistant Professor, Department of Nutrition, School of Medicine, The Univesity, 医学部, 助手 (40108866)
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| Project Period (FY) |
1986 – 1987
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| Project Status |
Completed (Fiscal Year 1987)
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| Budget Amount *help |
¥1,700,000 (Direct Cost: ¥1,700,000)
Fiscal Year 1987: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1986: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | Dimethylarginines / N^G ,N^G -dimetylarginine / N^G ,N'^G -dimethylarginine / metabolism / rats / citrulline dimethylarginine aminotransferase / ラット / 1-アミノプロリン / 【N^G】,【N^G】-ジメチルアルギニン / 【N^G】,【N^('G)】-ジメチルアルギニン / α-ケト-δ-(N,N-ジメチルグアニジノ)吉草酸 / α-ケト-δ-(N,N'-ジメチルグアニジノ)吉草酸 / 代謝 |
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| Research Abstract |
N^G,N^G - and N^G,N'^G -Dimethylarginine (DMA and DM'A) occur in natural proteins methylated post-translationally. Some investigators proposed to use these amino acids as an index of protein turnover in a similar manner to N^<<tau>> methylhistidine, without detailed metabolic studies. By our experiments, however, it was proved that these dimethylarginines were definitely metabolized in rats. Both DMA and DM'A were converted to N^<alpha> -acetyl conjugates and to -keto acids by unique aminotransferase catalyzing the transamination between DMA (DM'A) and pyruvate. In addition, the oxidatively decarboxylated products of the -keto acids were also found as the metabolites. Moreover, it was shown that DMA was catabolized to L-citrulline and other amino acids metabolically related to urea cycle. We found a novel enzyme responsible for the metabolic process of DMA, which catalizes the direct conversion of DMA to L-citrulline with hydrolytic liberation of dimethylamine from the methylated guanidino moiety of DMA. These enzymes were purified from rat kidney and were fully characterized as new enzymes.
These findings shows that the attempt to use the above-mentioned dimethyl-arginines as an index of in vivo protein breakdown is inadeqate at least in rats.
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