| Project/Area Number |
24510296
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Living organism molecular science
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| Research Institution | Nara Women's University |
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Principal Investigator |
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2014: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2012: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
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| Keywords | タンパク質の翻訳後修飾 / プロテオミクス / 末端基の修飾 / ケミカルバイオロジー / 化学修飾 / 同位体交換 / 同位体標識 / 質量分析 / アミノ酸配列解析 / 末端プロテオミクス / タンパク質考古学 / アスパラギンの脱アミド化 / イソペプチド / タンパク質分解酵素 / 末端アミノ酸配列解析 / タンパク質の化学修飾 / 考古学 / タンパク質科学 |
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| Outline of Final Research Achievements |
In order to identify mature proteins in which either N- or C-terminus is blocked, a new method for the modification of terminal free amino and carboxyl groups was developed. This method employs reagents containing the tris(trimethoxyphenyl)phosphonium (TMPP) group. In matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS), the TMPP reagents make it possible to detect the derivatized peptides at a greatly enhanced sensitivity, so that the N- and C-terminal sequencing with MALDI-MS can be performed with almost the same sensitivity. In the present study, a new reaction that converts the N-terminal aspartic acid residue to alanine or pyruvate through decarboxylation and subsequent deamination, respectively, was discovered. The possibility of developing a new method that uses this reaction was also pursued. This method was successfully applied to Egyptian archaeological specimens, which dated to 2,400 BG, thereby collagen derived from cow hide could be identified.
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