Quantification of stress-induced modification of serum protein using amine-reactive isotpe tags
Project/Area Number |
25460684
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Laboratory medicine
|
Research Institution | University of the Ryukyus (2014-2015) Shiga University of Medical Science (2013) |
Principal Investigator |
|
Project Period (FY) |
2013-04-01 – 2016-03-31
|
Project Status |
Completed (Fiscal Year 2015)
|
Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2015: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
|
Keywords | 翻訳後修飾 / ダブシルクロリド / アミノ酸 / 質量分析 / 安定同位体ラベル / キャピラリークロマトグラフィー / 微量分析 / メタボロミクス / 血清タンパク質 / 液体クロマトグラフィー / 血清アルブミン / 比較定量 |
Outline of Final Research Achievements |
Newly synthesized proteins consist mainly of 20 proteinogenic amino acids. However, in the biological environments, proteins are chemically modified both by physiological mechanisms such as phosphorylation/dephosphorylation and by reaction with highly reactive compounds such as reactive oxygen species and glucose. Irreversible modifications are more heavily accumulated on the relevant proteins when higher biological stress exists. Therefore, it is clinically important to measure accurately protein modification. In the present study, I aimed to quantify non-proteinogenic amino acids released from proteins by acid hydrolysis. Dabsyl groups with mass difference of 6 were used to discriminate amino acids derived from distinct samples. On the basis of capillary chromatography on a reverse-phase column combined with a conventional electrospray ion-trap mass spectrometer, the basics of simultaneous measurement of three samples has been established.
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Report
(4 results)
Research Products
(21 results)