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Developments in Mass Spectrometry for Glycosaminoglycan Analysis: A Review

This review covers recent developments in glycosaminoglycan (GAG) analysis via mass spectrometry (MS). GAGs participate in a variety of biological functions, including cellular communication, wound healing, and anticoagulation, and are important targets for structural characterization. GAGs exhibit...

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Detalles Bibliográficos
Autores principales: Pepi, Lauren E., Sanderson, Patience, Stickney, Morgan, Amster, I. Jonathan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8724624/
https://www.ncbi.nlm.nih.gov/pubmed/32938749
http://dx.doi.org/10.1074/mcp.R120.002267
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author Pepi, Lauren E.
Sanderson, Patience
Stickney, Morgan
Amster, I. Jonathan
author_facet Pepi, Lauren E.
Sanderson, Patience
Stickney, Morgan
Amster, I. Jonathan
author_sort Pepi, Lauren E.
collection PubMed
description This review covers recent developments in glycosaminoglycan (GAG) analysis via mass spectrometry (MS). GAGs participate in a variety of biological functions, including cellular communication, wound healing, and anticoagulation, and are important targets for structural characterization. GAGs exhibit a diverse range of structural features due to the variety of O- and N-sulfation modifications and uronic acid C-5 epimerization that can occur, making their analysis a challenging target. Mass spectrometry approaches to the structure assignment of GAGs have been widely investigated, and new methodologies remain the subject of development. Advances in sample preparation, tandem MS techniques (MS/MS), online separations, and automated analysis software have advanced the field of GAG analysis. These recent developments have led to remarkable improvements in the precision and time efficiency for the structural characterization of GAGs.
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spelling pubmed-87246242022-01-11 Developments in Mass Spectrometry for Glycosaminoglycan Analysis: A Review Pepi, Lauren E. Sanderson, Patience Stickney, Morgan Amster, I. Jonathan Mol Cell Proteomics Review This review covers recent developments in glycosaminoglycan (GAG) analysis via mass spectrometry (MS). GAGs participate in a variety of biological functions, including cellular communication, wound healing, and anticoagulation, and are important targets for structural characterization. GAGs exhibit a diverse range of structural features due to the variety of O- and N-sulfation modifications and uronic acid C-5 epimerization that can occur, making their analysis a challenging target. Mass spectrometry approaches to the structure assignment of GAGs have been widely investigated, and new methodologies remain the subject of development. Advances in sample preparation, tandem MS techniques (MS/MS), online separations, and automated analysis software have advanced the field of GAG analysis. These recent developments have led to remarkable improvements in the precision and time efficiency for the structural characterization of GAGs. American Society for Biochemistry and Molecular Biology 2021-01-06 /pmc/articles/PMC8724624/ /pubmed/32938749 http://dx.doi.org/10.1074/mcp.R120.002267 Text en © 2021 The Authors https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Pepi, Lauren E.
Sanderson, Patience
Stickney, Morgan
Amster, I. Jonathan
Developments in Mass Spectrometry for Glycosaminoglycan Analysis: A Review
title Developments in Mass Spectrometry for Glycosaminoglycan Analysis: A Review
title_full Developments in Mass Spectrometry for Glycosaminoglycan Analysis: A Review
title_fullStr Developments in Mass Spectrometry for Glycosaminoglycan Analysis: A Review
title_full_unstemmed Developments in Mass Spectrometry for Glycosaminoglycan Analysis: A Review
title_short Developments in Mass Spectrometry for Glycosaminoglycan Analysis: A Review
title_sort developments in mass spectrometry for glycosaminoglycan analysis: a review
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8724624/
https://www.ncbi.nlm.nih.gov/pubmed/32938749
http://dx.doi.org/10.1074/mcp.R120.002267
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