| Project/Area Number |
14572189
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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 |
Laboratory medicine
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| Research Institution | Osaka Medical College |
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Principal Investigator |
SHIMIZU Akira Osaka Medical College, Faculty of Medicine, Assistant, 医学部, 教授 (00028581)
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| Co-Investigator(Kenkyū-buntansha) |
MIYAZAKI Ayako Osaka Medical College, Faculty of Medicine, Assistant, 医学部, 助手 (20298772)
NAKANISHI Toyofumi Osaka Medical College, Faculty of Medicine, Lecturer, 医学部, 講師 (10247843)
岸川 匡彦 大阪医科大学, 医学部, 助手 (40268199)
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| Project Period (FY) |
2002 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 2003: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2002: ¥2,200,000 (Direct Cost: ¥2,200,000)
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| Keywords | Modified Protein / Sulfite Oxidase / Transthyretin / Mass Spectrometry / Electrospray / Immunoprecipitation / Homocysteine / Molybdenum cofactor deficiency / 質量分析 |
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| Research Abstract |
Cysteine and cystine in protein are modified to various derivatives in vitro and in vivo. By electrospray ionization mass spectrometry (ESI-MS), we found derivatives of serum transthyretin (TTR) in which cysteine residue at position 10 was changed to glycine residue and sulfocysteine residue. The change, cysteine to glycine, was unique and the origin of the sulfonic acid group was controversial. In the present paper, we show the molecular masses of various TTR derivatives including these two, and the modification process was studied using a synthetic peptide with the same sequence as cysteine containing part of TTR, i.e., SKCPLMVK. After incubation of the peptide at pH 8.3, various derivatives were generated, which showed changes of cysteine residue to glycine, dehydroalanine, S-thiocysteine, and S-sulfocysteine residues, which were confirmed by molecular mass and collision-induced dissociation spectra. Dehydroalanine may react with other amino acids and contribute to form cross-linking fibril, causing amyloidosis.
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