A method to identify glycan sequencing based on tandem mass spectrometry

• Main Authors: Chun-Lin Huang, 黃群霖
• Other Authors: Tzong-Yi Lee
• Format: Others
• Language: zh-TW
• Published: 2016
• Online Access: http://ndltd.ncl.edu.tw/handle/yzmbnb

碩士 === 元智大學 === 資訊工程學系 === 104 === N-linked Glycosylation is an important post-translational modification. More than 50% of eukaryotic proteins are glycosylated. Clinical trials have shown that abnormal glycosylation affects cancer progression, malignancy and immune response. Tandem mass spectrometry have better selectivity and sensitivity, and can provide high throughput information. In this study, we developed a TMSeq software system for the analysis of glycan structure and peptides sequence from Intact N-linked glycopeptides by mass spectrometry analysis. The system uses collision-induced dissociation (CID) and higher-energy collisional dissociation (HCD) peak signal to analyze potential N-link glycosylation spectrums. The system also provides a visual interface, processes high throughput spectrum information, and record detailed spectrum results for users. The results of TMSeq analysis have identified glycan structure in AFP standard and patients with liver cancer.