Heat-Induced Rearrangement of the Disulfide Bond of Lactoglobulin Characterized by Multiply Charged MALDI-TOF/TOF Mass Spectrometry
文献类型：期刊论文
| 作者 | Zhan, Lingpeng1,2; Liu, Yu2; Xie, Xiaobo1,2; Xiong, Caiqiao1; Nie, Zongxiu1,3 |
| 刊名 | ANALYTICAL CHEMISTRY
 |
| 出版日期 | 2018-09-18 |
| 卷号 | 90期号:18页码:10670-10675 |
| ISSN号 | 0003-2700 |
| DOI | 10.1021/acs.analchem.8b02563 |
| 英文摘要 | Disulfide bonds are an important post-translational modification of proteins and play a significant role in stabilizing protein structure. While both mass spectrometry-based bottom-up and top-down proteomics are widely used in the identification of disulfide linkages, the top-down approach can avoid potential information loss of disulfide linkage occurring in the bottom-up analysis. In the present work, we applied matrix-assisted laser desorption/ionization tandem Time-of-Flight (MALDI-TOF/TOF) mass spectrometry to investigate the heat-induced disulfide rearrangement of beta-lactoglobulin (beta-LG). Since beta-LG (18 kDa) is too large for common TOF/TOF analysis, we use 2-nitrophloroglucinol (2-NPG) as a matrix to generate multiply charged proteins by MALDI. Fragmentation of doubly charged protein ions yields characteristic triplet peaks of disulfide bonds. We found that the characteristic fragments derived from the heterolytic cleavage of disulfide bonds decreased sharply when the incubation temperature of beta-LG solution reached the critical point of 75 degrees C. These results indicate that the disulfide linkage between C160 and C66 has been broken during the heating process and, probably, new disulfide formed. In conclusion, our work highlights the analytical value of the multiply charged MALDI-TOF/TOF method in the identification of larger proteins (>12 kDa) and disulfide-containing proteins. |
| 语种 | 英语 |
| 出版者 | AMER CHEMICAL SOC |
| WOS记录号 | WOS:000445322800007 |
| 源URL | [http://ir.iccas.ac.cn/handle/121111/43025]  |
| 专题 | 中国科学院化学研究所 |
| 通讯作者 | Nie, Zongxiu |
| 作者单位 | 1.Chinese Acad Sci, Inst Chem, Beijing Natl Lab Mol Sci, Key Lab Analyt Chem Living Biosyst, Beijing 100190, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 3.Natl Ctr Mass Spectrometry Beijing, Beijing 100190, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhan, Lingpeng,Liu, Yu,Xie, Xiaobo,et al. Heat-Induced Rearrangement of the Disulfide Bond of Lactoglobulin Characterized by Multiply Charged MALDI-TOF/TOF Mass Spectrometry[J]. ANALYTICAL CHEMISTRY,2018,90(18):10670-10675. |
| APA | Zhan, Lingpeng,Liu, Yu,Xie, Xiaobo,Xiong, Caiqiao,&Nie, Zongxiu.(2018).Heat-Induced Rearrangement of the Disulfide Bond of Lactoglobulin Characterized by Multiply Charged MALDI-TOF/TOF Mass Spectrometry.ANALYTICAL CHEMISTRY,90(18),10670-10675. |
| MLA | Zhan, Lingpeng,et al."Heat-Induced Rearrangement of the Disulfide Bond of Lactoglobulin Characterized by Multiply Charged MALDI-TOF/TOF Mass Spectrometry".ANALYTICAL CHEMISTRY 90.18(2018):10670-10675. |
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来源：化学研究所
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