Quantitative characterization of intact sialylated O-glycans with MALDI-MS for protein biotherapeutics
- Authors
- Hwang, C.-H.; Park, H.-M.; Park, H.-G.; Ahn, D.-H.; Kim, S.-M.; Ko, B.J.; Kim, Y.H.; Yang, Y.-H.; Kim, Y.-G.
- Issue Date
- Jul-2018
- Publisher
- Springer New York LLC
- Keywords
- Chemical Derivatization; MALDI-MS; O-glycan; Protein Biotherapeutics; Quantitative Analysis
- Citation
- Korean Journal of Chemical Engineering, v.35, no.7, pp.1462 - 1467
- Journal Title
- Korean Journal of Chemical Engineering
- Volume
- 35
- Number
- 7
- Start Page
- 1462
- End Page
- 1467
- URI
- http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/31508
- DOI
- 10.1007/s11814-018-0058-0
- ISSN
- 0256-1115
- Abstract
- For validating O-glycosylation of protein biotherapeutics, we presented a quantitative O-glycomics method which is based on the neutralization of sialic acids, the specific release of O-glycans, and the introduction of permanent positive charge followed by quantitative MALDI-MS analysis. This method shows excellent technical reproducibility, linearity and sensitivity. In addition, it enables the quantification of intact O-glycans with minimal degradation or loss of sialic acids on these glycans compared to a conventional HPLC-based method. We then applied this method to quantitatively characterize O-glycans present on Etanercept. The analysis showed the relative abundances of mono- and di-sialylated core 1 O-glycans - were 79.3±0.8% and 17.3±1.4%, respectively. This glycomics technology could allow for the reliable quantitative analysis of intact O-glycans from glycoproteins and may contribute to validation of O-glycosylation protein biotherapeutics in the pharmaceutical industry. © 2018, Korean Institute of Chemical Engineers, Seoul, Korea.
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