| Project/Area Number |
59440077
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| Research Category |
Grant-in-Aid for General Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
Functional basic dentistry
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| Research Institution | TOHOKU UNIVERSITY |
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Principal Investigator |
YAMADA Tadashi Professor, Tohoku University School of Dentistry, 歯学部, 教授 (50005021)
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| Co-Investigator(Kenkyū-buntansha) |
IWAMI Yoshimichi Research Associate, Tohoku University School of Dentistry, 歯学部, 助手 (60005030)
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| Project Period (FY) |
1984 – 1986
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| Project Status |
Completed (Fiscal Year 1986)
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| Budget Amount *help |
¥14,000,000 (Direct Cost: ¥14,000,000)
Fiscal Year 1986: ¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 1985: ¥2,500,000 (Direct Cost: ¥2,500,000)
Fiscal Year 1984: ¥10,000,000 (Direct Cost: ¥10,000,000)
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| Keywords | Anaerobic metabolism / Sugar metabolism / Streptococcus sanguis / Streptococcus mutans / Pyruvate formate-lyase / 酵素の型変換 / 酵素の酸素感受性 / フッ素 / 口腔レンサ球菌 / 糖代謝 / 酸素感受性酵素 / 歯垢 / 酸産生 |
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| Research Abstract |
The acids generated through the fermentation of sugar by the microorganisms in dental plaque are directly involved in the initiation and progression of dental caries. The sugar metabolism by these microorganisms is also affected greatly by the contact of the organisms to air. The environmental conditions in dental plaque vary greatly during the cycle of the daily life, especially by meals. Thus, we studied the biochemical mechanism of the recovery of the sugar metabolism from the impairment by oxygen.
We found that the sugar metabolism of Streptococcus mutans was more sensitive than that of Streptococcus sanguis. The low sensitivity of the sugar metabolism of S. sanguis stems from the interconversion of pyruvate formate-lyase between the two forms of this enzyme, while S. mutans cannot do this interconversion. The active pyruvate formate-lyase converted into an inactive form of the enzyme(R-form) when the intact cells were incubated anaerobically without sugar. The R-form enzyme was reactivated in the cells when sugar was available under strictly anaerobic conditions. The R-form of the enzyme was not sensitive to oxygen, while the active enzyme was extremely sensitive. The contact to oxygen converted the active enzyme into another form of an inactive enzyme that was not reactivated. The intact cells of S. mutans had no such a system to convert an active enzyme into the R-form. This could be a reason why S. mutans is sensitive to oxygen.
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