A Method for Mapping Glycosylation Sites in Proteins

Han, Mark; Simpson, John T.

doi:10.7171/jbt.17-2804-001

Cited by 3 publications

(2 citation statements)

References 12 publications

(5 reference statements)

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“…This allows for difficult to digest proteins to be digested without the use of typical reduction and alkylation steps. 19 Additionally, the resin-bound proteases allow for quick clean up via a solid phase extraction or centrifugal filter procedure. Overall, trypsin digestion occurs within one hour reducing the time it takes to conduct a typically laborious trypsin digestion 45 .…”

Section: Advances In Mab Denaturation and Deglycosylation Methodsmentioning

confidence: 99%

Recent Advances in Biologic Therapeutic N-Glycan Preparation Techniques and Analytical Methods for Facilitating Biomanufacturing Automation

Tiwold

Gyorgypal

Chundawat

2023

Journal of Pharmaceutical Sciences

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Section: Advances In Mab Denaturation and Deglycosylation Methodsmentioning

confidence: 99%

Recent Advances in Biologic Therapeutic N-Glycan Preparation Techniques and Analytical Methods for Facilitating Biomanufacturing Automation

Tiwold

Gyorgypal

Chundawat

2023

Journal of Pharmaceutical Sciences

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“…ZIC‐HILIC was applied for the separation of non‐sialylated moieties successfully . Similar glycopeptides from IgG1, IgG2, and IgG4 were finely separated on Glycan BEH Amide , TSKgel Amide‐80 , and Halo Penta‐HILIC . Sialylated glycopeptides on EEQYNSTYR and EEQFNSTFR were analyzed by Drop‐HILIC enrichment, followed by RPLC–ESI–MS/MS .…”

Section: Analysis Of N‐ and O‐glycopeptidesmentioning

confidence: 99%

Hydrophilic interaction chromatography for the analysis of biopharmaceutical drugs and therapeutic peptides: A review based on the separation characteristics of the hydrophilic interaction chromatography phases

Ikegami

2019

J of Separation Science

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Applications of hydrophilic interaction chromatography for the analysis of biopharmaceutical drugs, i.e., glycosylated proteins represented by monoclonal antibodies are discussed in the manner of glycoproteomics. They can be analyzed using hydrophilic interaction chromatography in five different stages as (1) their intact forms, (2) their subunits, (3) N‐ and O‐glycopeptides digested by proteases, (4) N‐ and O‐glycans released from the glycoproteins or glycopeptides, and (5) monosaccharides. Hydrophilic interaction chromatography is a more useful tool in the order of (1) to (5). At the stages (4) and (5), quantitation of glycans and saccharides are also reported. Hydrophilic interaction chromatography is employed not only for analytical uses, but also pretreatment items as solid phase extraction, followed by reversed‐phase liquid chromatography separations. Comprehensive search results of these application of hydrophilic interaction chromatography are summarized in tables to show what kind of hydrophilic interaction chromatography columns are suitable for each step of analysis.Relationship of favored and less favored hydrophilic interaction chromatography columns and their separation characteristics such as hydrophilicity, and selectivity for structural difference, is also discussed. Analysis of the therapeutic peptides (not glycosylated) using hydrophilic interaction chromatography is summarized, too.

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Hydrophilic interaction liquid chromatography-mass spectrometry for the characterization of glycoproteins at the glycan, peptide, subunit, and intact level

Gargano

Haselberg

Somsen

2021

Carbohydrate Analysis by Modern Liquid Phase Separation Techniques

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A Method for Mapping Glycosylation Sites in Proteins

Cited by 3 publications

References 12 publications

Recent Advances in Biologic Therapeutic N-Glycan Preparation Techniques and Analytical Methods for Facilitating Biomanufacturing Automation

Recent Advances in Biologic Therapeutic N-Glycan Preparation Techniques and Analytical Methods for Facilitating Biomanufacturing Automation

Hydrophilic interaction chromatography for the analysis of biopharmaceutical drugs and therapeutic peptides: A review based on the separation characteristics of the hydrophilic interaction chromatography phases

Hydrophilic interaction liquid chromatography-mass spectrometry for the characterization of glycoproteins at the glycan, peptide, subunit, and intact level

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