| Project/Area Number |
11650814
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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 |
生物・生体工学
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| Research Institution | Yamanashi University |
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Principal Investigator |
AMANO Yoshifumi Yamanashi Univ., Fac. Eng., Professor, 工学部, 教授 (70020401)
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| Co-Investigator(Kenkyū-buntansha) |
NAKAMURA Kazuo Yamanashi Univ., Fac. Eng., Assistant, 工学部, 助手 (80111780)
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| Project Period (FY) |
1999 – 2000
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| Project Status |
Completed (Fiscal Year 2000)
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| Budget Amount *help |
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 2000: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1999: ¥1,800,000 (Direct Cost: ¥1,800,000)
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| Keywords | ATP / ATPase / cytochrome c / cytochrome c oxidase / acid resistant / sulfur oxidizing bacteria / シトクロムc / シトクロムc酸化酵素 / シトクロム【C!_】 |
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| Research Abstract |
Thiobacillus thiooxidans, sulfur-oxidizing bacteria with acid resistance, acquires energy (ATP) with the help of the pH gap of extracellar pH (low) and intracellar pH (neutral). The acid-resistant factors in the bacteria seem to be cytochrome c and H^+-ATPase which is ATP synthetase. In this study, these acid-resistant factor were separated, and the property was examined.
Cytochrome c : Cell-free extract of bacteria was divided by centrifugation into membrane fraction and water-soluble fraction. Membrane -bound cytochrome c which existed in the membrane fraction was the basic protein, and the molecular weight was 18 kDa, and the isoelectric point was 8.2. The molecular weight of water-soluble cytochrome c was 10.1 kDa. The reduced cytochrome c had the absorption spectrum for 416.5, 522, and 551 nm. The oxidized cytochrome c had the absorption spectrum for 409.5 nm. The isoelectric point was 8.5. H^+-ATPase : ATPase which existed in the cell membrane was the F_0F_1 type. The optimum activity of ATPase was observed in the decomposition of ATP at pH8.0, 60℃. The activity increased with increasing Mg^<2+> concentration, and it became a maximum at 4 mM-Mg^<2+>. As a characteristic property in ATPase of T.thiooxidans, the ATP decomposing activity was dependent on the sulfurous acid (SO_3^<2->) concentration.
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