| Project/Area Number |
01580192
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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 |
代謝生物化学
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| Research Institution | Shimane Medical University |
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Principal Investigator |
SHIMOYAMA Makoto Shimane Med. Univ., Dept. of Bio chem., Prof., 医学部, 教授 (30084859)
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| Co-Investigator(Kenkyū-buntansha) |
TERASHIMA Masaharu Shimane Med. Univ., 医学部, 助手 (40227517)
OBARA Seiji Shimane Med. Univ., 医学部, 助手 (70204279)
MISHIMA Koichi Shimane Med. Univ., 医学部, 講師 (90181875)
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| Project Period (FY) |
1989 – 1990
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| Project Status |
Completed (Fiscal Year 1990)
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| Budget Amount *help |
¥1,900,000 (Direct Cost: ¥1,900,000)
Fiscal Year 1990: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1989: ¥1,400,000 (Direct Cost: ¥1,400,000)
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| Keywords | mono (ADP-ribose) / NAD / ADP-ribosyltransferase / skeletal muscle SR / posttranslational modification / SR membrane / arginine / モノ(ADP-リボ-ス) / 後翻訳修飾 |
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| Research Abstract |
Arginine-specific mono (ADP-ribosyl) transference in rabbit skeletal muscle sarcoplasmic reticulum (SR) was investigated. The enzyme solubilized with 1% Triton X-100 from the SR membranes was purified and characterized. Trypsin also solubilized the transference as active form. The properties including the molecular sizes of the trypsin-solubilized enzyme resemble those of the Triton-solubilized enzyme. These results indicate that just one part of the transference may be inserted in the SR membrane.
Studies on distribution of the transference in chickens showed the highest specific activity in peripheral polymorphonuclear cells (heterophils). Purification and characterization of the heterophil enzyme revealed that the properties were indistinguishable from those of the liver enzyme, but those were different between chicken liver and rabbit SR enzymes. For example, dithiothreitol, which activate the liver enzyme, inhibited the SR enzyme. The physiological role of endogenous transference remains obscure, presumably because much less is known of acceptor proteins for the enzyme. We identified and characterized them ; Ca^<2+> -ATPase in rabbit skeletal muscle SR and 33 kDa protein (p33) in chicken liver. Chicken heterophils also contained high levels of p33. The SR transference did not modify the p33 and the liver enzyme did not ADP-ribosylate the ATPase. These results suggest that species, tissue and cell-specific ADP-ribosyltransferases prefer their own target proteins for the in situ ADP-ribosylation.
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