Glycan analysis of therapeutic glycoproteins
Therapeutic monoclonal antibodies (mAbs) are glycoproteins produced by living cell systems. The glycan moieties attached to the proteins can directly affect protein stability, bioactivity, and immunogenicity. Therefore, glycan variants of a glycoprotein product must be adequately analyzed and contro...
| Main Authors: | , , |
|---|---|
| Format: | Online |
| Language: | English |
| Published: |
Taylor & Francis
2015
|
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4966609/ |
| id |
pubmed-4966609 |
|---|---|
| recordtype |
oai_dc |
| spelling |
pubmed-49666092016-08-24 Glycan analysis of therapeutic glycoproteins Zhang, Lei Luo, Shen Zhang, Baolin Review Therapeutic monoclonal antibodies (mAbs) are glycoproteins produced by living cell systems. The glycan moieties attached to the proteins can directly affect protein stability, bioactivity, and immunogenicity. Therefore, glycan variants of a glycoprotein product must be adequately analyzed and controlled to ensure product quality. However, the inherent complexity of protein glycosylation poses a daunting analytical challenge. This review provides an update of recent advances in glycan analysis, including the potential utility of lectin-based microarray for high throughput glycan profiling. Emphasis is placed on comparison of the major types of analytics for use in determining unique glycan features such as glycosylation site, glycan structure, and content. Taylor & Francis 2015-11-24 /pmc/articles/PMC4966609/ /pubmed/26599345 http://dx.doi.org/10.1080/19420862.2015.1117719 Text en This article not subject to US copyright law. http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Zhang, Lei Luo, Shen Zhang, Baolin |
| spellingShingle |
Zhang, Lei Luo, Shen Zhang, Baolin Glycan analysis of therapeutic glycoproteins |
| author_facet |
Zhang, Lei Luo, Shen Zhang, Baolin |
| author_sort |
Zhang, Lei |
| title |
Glycan analysis of therapeutic glycoproteins |
| title_short |
Glycan analysis of therapeutic glycoproteins |
| title_full |
Glycan analysis of therapeutic glycoproteins |
| title_fullStr |
Glycan analysis of therapeutic glycoproteins |
| title_full_unstemmed |
Glycan analysis of therapeutic glycoproteins |
| title_sort |
glycan analysis of therapeutic glycoproteins |
| description |
Therapeutic monoclonal antibodies (mAbs) are glycoproteins produced by living cell systems. The glycan moieties attached to the proteins can directly affect protein stability, bioactivity, and immunogenicity. Therefore, glycan variants of a glycoprotein product must be adequately analyzed and controlled to ensure product quality. However, the inherent complexity of protein glycosylation poses a daunting analytical challenge. This review provides an update of recent advances in glycan analysis, including the potential utility of lectin-based microarray for high throughput glycan profiling. Emphasis is placed on comparison of the major types of analytics for use in determining unique glycan features such as glycosylation site, glycan structure, and content. |
| publisher |
Taylor & Francis |
| publishDate |
2015 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4966609/ |
| _version_ |
1613617830233636864 |