A MALDI-MS-based quantitative targeted glycomics (MALDI-QTaG) for total N-glycan analysis
- Authors
- Kim, Kyoung-Jin; Kim, Yoon-Woo; Hwang, Cheol-Hwan; Park, Han-Gyu; Yang, Yung-Hun; Koo, Miyoung; Kim, Yun-Gon
- Issue Date
- Oct-2015
- Publisher
- SPRINGER
- Keywords
- Abnormal glycosylation; Chemical derivatization; MALDI-MS; N-Glycan; Glycosylation; Quantitative analysis; UPLC
- Citation
- BIOTECHNOLOGY LETTERS, v.37, no.10, pp.2019 - 2025
- Journal Title
- BIOTECHNOLOGY LETTERS
- Volume
- 37
- Number
- 10
- Start Page
- 2019
- End Page
- 2025
- URI
- http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/8627
- DOI
- 10.1007/s10529-015-1881-6
- ISSN
- 0141-5492
- Abstract
- To develop a sensitive and quantitative method for monitoring the abnormal glycosylation of clinical and biopharmaceutical products. MALDI-MS-based quantitative targeted glycomics (MALDI-QTaG) was proposed for sensitive and quantitative analysis of total N-glycans. The derivatization reactions (i.e., amidation of sialic acid and incorporation of a positive charge moiety into the reducing end) dramatically increased the linearity (R-2 > 0.99) and sensitivity (limit of detection is 0.5 pmol/glycoprotein) relative to underivatized glycans. In addition, the analytical strategy was chromatographic purification-free and non-laborious process accessible to the high-throughput analyses. We used MALDI-QTaG to analyze the N-glycans of alpha-fetoprotein (AFP) purified from normal cord blood and HCC cell line (Huh7 cells). The total percentages of core-fucosylated AFP N-glycans from Huh7 cells and normal cord blood were 98 and 18 %, respectively. This MALDI-MS-based glycomics technology has wide applications in many clinical and bioengineering fields requiring sensitive, quantitative and fast N-glycosylation validation.
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