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- W2756221472 endingPage "1383" @default.
- W2756221472 startingPage "1373" @default.
- W2756221472 abstract "Aim: Glycosylation of recombinant human erythropoietins (rhEPOs) is significantly associated with drug's quality and potency. Thus, comprehensive characterization of glycosylation is vital to assess the biotherapeutic quality and establish the equivalency of biosimilar rhEPOs. However, current glycan analysis mainly focuses on the N-glycans due to the absence of analytical tools to liberate O-glycans with high sensitivity. We developed selective and sensitive method to profile native O-glycans on rhEPOs. Results: O-glycosylation on rhEPO including O-acetylation on a sialic acid was comprehensively characterized. Details such as O-glycan structure and O-acetyl-modification site were obtained from tandem MS. Conclusion: This method may be applied to QC and batch analysis of not only rhEPOs but also other biotherapeutics bearing multiple O-glycosylations." @default.
- W2756221472 created "2017-09-25" @default.
- W2756221472 creator A5002177286 @default.
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- W2756221472 date "2017-09-01" @default.
- W2756221472 modified "2023-09-26" @default.
- W2756221472 title "Sensitive and comprehensive analysis of <i>O</i>-glycosylation in biotherapeutics: a case study of novel erythropoiesis stimulating protein" @default.
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- W2756221472 doi "https://doi.org/10.4155/bio-2017-0085" @default.
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