Development of a high performance anion exchange chromatography analysis for mapping of oligosaccharides

Grey, Carl; Edebrink, Per; Krook, Maria; Jacobsson, Sven P.

doi:10.1016/j.jchromb.2009.05.003

Cited by 42 publications

(20 citation statements)

References 27 publications

(32 reference statements)

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“…However, relative PAD response is an excellent quantitative approximation for glycans with fairly similar structures [26,55,56,60,61,78,79,84], and this is the case here for IgG neutral diantennary N-glycans. …”

Section: Separation and Detection Of Saccharides By Hpaec-padmentioning

confidence: 76%

Comparison of orthogonal chromatographic and lectin-affinity microarray methods for glycan profiling of a therapeutic monoclonal antibody

Cook

Kaldas

Muradia

et al. 2015

Journal of Chromatography B

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Section: Separation and Detection Of Saccharides By Hpaec-padmentioning

confidence: 76%

Comparison of orthogonal chromatographic and lectin-affinity microarray methods for glycan profiling of a therapeutic monoclonal antibody

Cook

Kaldas

Muradia

et al. 2015

Journal of Chromatography B

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“…Isomer Separation and Quantitation of Cell Surface Glycans-Glycan composition can be readily obtained based solely on MALDI-FT-ICR MS, and the abundances can also be determined with reasonable precision using peak intensities if the homogeneity of the sample surface can be guaranteed with the proper matrix (37,38). However, this analysis does not provide information on the number of isomers associated with the compositions.…”

Section: Resultsmentioning

confidence: 99%

Extensive Determination of Glycan Heterogeneity Reveals an Unusual Abundance of High Mannose Glycans in Enriched Plasma Membranes of Human Embryonic Stem Cells

Gip

Kim

et al. 2012

Molecular & Cellular Proteomics

103

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Glycosylation is the process by which oligosaccharides, termed glycans, are appended onto membrane and secreted proteins and lipids. It is the most common and complex form of post-translational modification, with ϳ50% of all eukaryotic proteins glycosylated (1, 2). A majority of glycans are found on the cell surface, where they are optimally poised to be the first cellular components encountered by approaching cells, pathogens, antibodies, or other molecules, as well as advertise information about the internal state and homeostasis of the cell (3, 4). Therefore, glycans play an essential role in many biological processes, including cell development and differentiation, cell-cell or cell-matrix communication, and pathogen-host recognition (3,(5)(6)(7). In fact, differences in glycan profiles between healthy and diseased states are utilized for clinical diagnosis (7), providing targets for many novel classes of therapeutics including cancer chemotherapy, diabetes treatment, and antibiotic and anti-viral medicine (5, 8). Glycans are highly heterogeneous in nature, varying in the composition of individual monosaccharide building blocks, the positions with which these building blocks link to each other, and the stereochemical disposition of the linkages (␣ or ␤). This complexity has presented a significant challenge for obtaining structural information about glycans at the molecular From the

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“…Increasing glycan size and sialylation is believed to cause reduction in PAD response. 68,69 This might account for the small differences for G0F and the sialylated species.…”

Section: Discussionmentioning

confidence: 99%

Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles—Part 1: Separation-based methods

Reusch

Haberger

Maier

et al. 2015

mAbs

146

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(2015) Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles-Part 1: Separation-based methods, mAbs, 7:1, 167-179, DOI: 10.4161/19420862.2014.986000 To link to this article: https://doi.org/10. 4161/19420862.2014 Abbreviations: mAb, monoclonal antibody; Fc, fragment crystallizable; IgG, immunoglobulin G; HILIC-UPLC, hydrophilic interaction liquid chromatography-ultra high performance liquid chromatography; 2-AB, 2-aminobenzamide; Fab, fragment, antigen-binding; CE-LIF, capillary electrophoresis-laser induced fluorescence; HPLC, high performance liquid chromatography; MALDI-MS, matrix-assisted laser desorption/ionization-mass spectrometry; ESI-MS, electrospray ionization-mass spectrometry; HPAEC-PAD, high-performance anion exchange chromatography with pulsed amperometric detection; APTS, 8-aminopyrene-1, 3, 6-trisulfonic acid; DSA-FACE, DNA-sequencer-aided fluorophore-assisted carbohydrate electrophoresis; ANTS, 8-aminonaphthalene-1, 3, 6-trisulfonate; CCGE, cartridge-based capillary gel electrophoresis; HR, high resolution; IAB, InstantAB labeling; CHO, Chinese hamster ovaryImmunoglobulin G (IgG) crystallizable fragment (Fc) glycosylation is crucial for antibody effector functions, such as antibody-dependent cell-mediated cytotoxicity, and for their pharmacokinetic and pharmacodynamics behavior. To monitor the Fc-glycosylation in bioprocess development, as well as product characterization and release analytics, reliable techniques for glycosylation analysis are needed. A wide range of analytical methods has found its way into these applications. In this study, a comprehensive comparison was performed of separation-based methods for Fcglycosylation profiling of an IgG biopharmaceutical. A therapeutic antibody reference material was analyzed 6-fold on 2 different days, and the methods were compared for precision, accuracy, throughput and other features; special emphasis was placed on the detection of sialic acid-containing glycans. Seven, non-mass spectrometric methods were compared; the methods utilized liquid chromatography-based separation of fluorescent-labeled glycans, capillary electrophoresis-based separation of fluorescent-labeled glycans, or high-performance anion exchange chromatography with pulsed amperometric detection. Hydrophilic interaction liquid chromatography-ultra high performance liquid chromatography of 2-aminobenzamide (2-AB)-labeled glycans was used as a reference method. All of the methods showed excellent precision and accuracy; some differences were observed, particularly with regard to the detection and quantitation of minor glycan species, such as sialylated glycans.

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Development of a high performance anion exchange chromatography analysis for mapping of oligosaccharides

Cited by 42 publications

References 27 publications

Comparison of orthogonal chromatographic and lectin-affinity microarray methods for glycan profiling of a therapeutic monoclonal antibody

Comparison of orthogonal chromatographic and lectin-affinity microarray methods for glycan profiling of a therapeutic monoclonal antibody

Extensive Determination of Glycan Heterogeneity Reveals an Unusual Abundance of High Mannose Glycans in Enriched Plasma Membranes of Human Embryonic Stem Cells

Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles—Part 1: Separation-based methods

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