Multi-Level Characterization of Protein Glycosylation

Hua, Serenus; Oh, Myung Jin; An, Hyun Joo

doi:10.5478/msl.2013.4.1.10

Cited by 3 publications

(1 citation statement)

References 96 publications

(18 reference statements)

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“…Glycosylation is one of the most common forms of post‐translational modification . Glycans are the products of glycosylation and play a variety of structural and functional roles in membrane and secreted proteins . Matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry (MALDI‐TOF MS) is commonly used for the analysis and detection of glycans .…”

Section: Summary Of the Identified Glycans Obtained From Deglycosylatmentioning

confidence: 99%

Matrix Additives in MALDI‐TOF MS Analysis of Glycans

Kim

Shin

et al. 2015

Bulletin Korean Chem Soc

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Section: Summary Of the Identified Glycans Obtained From Deglycosylatmentioning

confidence: 99%

Matrix Additives in MALDI‐TOF MS Analysis of Glycans

Kim

Shin

et al. 2015

Bulletin Korean Chem Soc

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Enhanced Detection of Glycans by MALDI-TOF Mass Spectrometry Using a Binary Matrix of 2,5-Dihydroxybenzoic Acid and 2,6-Dihydroxybenzoic Acid

Kim¹,

Kim²,

Lee³

et al. 2013

Mass Spectrometry Letters

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Glycans released from ovalbumin by PNGase F were analyzed by matrix-assisted laser desorption/ionization time-offlight (MALDI-TOF) mass spectrometry using three different dihydroxybenzoic acid (DHB) matrix systems: 2,5-DHB, 2,6-DHB, and a 2,5-DHB/2,6-DHB binary matrix. Relative to the results obtained with the single-component matrices (2,5-DHB or 2,6-DHB), the 2,5-DHB/2,6-DHB binary matrix boasted lower background noise and higher sensitivity. A total of 16 glycan peaks were observed using the 2,5-DHB/2,6-DHB binary matrix, while only 10 and 9 glycan peaks were observed using the 2,5-DHB and 2,6-DHB matrices, respectively.

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MS Platform for Erythropoietin Glycome Characterization

Seo¹,

Kim²,

Oh³

et al. 2015

Mass Spectrometry Letters

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Recombinant erythropoietins (EPOs) are an important class of biotherapeutics that stimulate red blood cell production. The quality, safety, and potency of EPO variants are determined largely by their glycosylation, which makes up nearly half their mass. Thus, detailed glycomic analyses are important to assess biotherapeutic quality and establish the equivalency of biosimilar EPOs now coming to market. High-resolution mass spectrometry (MS) has recently emerged as the premier tool for glycan analysis in EPOs. Using the accurate mass measurements provided by high-resolution MS, the compositions of even large, complex glycans can easily be determined. When combined with a nano-LC separation, differentiation of structural isomers also becomes a possibility. These components, together, provide a comprehensive picture of biotherapeutic glycosylation. In this review, we provide an overview of MS-based analytical platform for glycomic characterization of EPO biotherapeutics and biosimilars.

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Multi-Level Characterization of Protein Glycosylation

Cited by 3 publications

References 96 publications

Matrix Additives in MALDI‐TOF MS Analysis of Glycans

Matrix Additives in MALDI‐TOF MS Analysis of Glycans

Enhanced Detection of Glycans by MALDI-TOF Mass Spectrometry Using a Binary Matrix of 2,5-Dihydroxybenzoic Acid and 2,6-Dihydroxybenzoic Acid

MS Platform for Erythropoietin Glycome Characterization

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