| Bulletin of the Korean chemical society | |
| Mass Spectrometry Analysis of In Vitro Nitration of Carbonic Anhydrase II | |
| Eugene C. Yi1  Mohammad Humayun Kabir1  Byungjoo Kim1  Jeong Won Kang1  Kyung Cho Cho1  Yong-Hyeon Yim1  Kwang Pyo Kim1  Hyoung Soon Park1  Soo Jae Lee1  | |
| 关键词: Mass spectrometry; FT-ICR MS; High resolution MS; Nitration; Nitrosylation; | |
| DOI : | |
| 学科分类:化学(综合) | |
| 来源: Korean Chemical Society | |
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【 摘 要 】
Protein tyrosine nitration is considered as an important indicator of nitrosative stresses and as one of the main factors for pathogenesis of inflammation and neuronal degeneration. In this study, we investigated various nitrosative modifications of bovine carbonic anhydrase II (CAII) through qualitative and semi-quantitative analysis using the combined strategy of Fourier transformation ion cyclotron resonance mass spectrometry (FT-ICR MS) and ion-trap tandem mass spectrometry (IT-MS/MS). FT-ICR MS and its spectra were used for the search of the pattern of nitrosative modifications. Identification of nitrosatively modified tyrosine sites were executed through IT-MS/MS. In addition, we also tried to infer the reason for the site-specific nitrosative modifications in CAII. In view of the above purpose, we have explored- i) the side chain accessibility, ii) the electrostatic environment originated from the acidic/basic amino acid residues neighboring to the nitrosatively modified site and iii) the existence of competing amino acid residues for nitration.
【 授权许可】
Unknown
【 预 览 】
| Files | Size | Format | View |
|---|---|---|---|
| RO201912010245038ZK.pdf | 1686KB |
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