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Analysis of glycoprotein heterogeneity by capillary electrophoresis and mass spectrometry

Hooker, Andrew D., James, David C. (2000) Analysis of glycoprotein heterogeneity by capillary electrophoresis and mass spectrometry. Molecular Biotechnology, 14 (3). pp. 241-249. ISSN 1073-6085. (doi:10.1385/MB:14:3:241) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:16233)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
http://dx.doi.org/10.1385/MB:14:3:241

Abstract

Glycosylation is a complex posttranslational modification that can result in extensive heterogeneity for recombinant glycoproteins produced by eukaryotic systems. The carbohydrate moiety of a recombinant glycoprotein may affect the immunogenicity, half-life, bioactivity, and stability of a potential therapeutic product. Regulatory authorities such as the US Food and Drug Administration demand increasingly sophisticated carbohydrate analysis to ensure product characterization, batch-to-batch consistency, and stability. The advent of new technologies for analysis of biopolymers by capillary electrophoresis and mass spectrometry has revolutionized strategies for recombinant protein characterization. In particular, recent advances in matrix-assisted laser desorption/ionization and electrospray ionization mass spectrometry now permit relatively rapid and detailed assessment of glycoprotein and oligosaccharide structure. In this article, we describe some applications of capillary electrophoresis and mass spectrometry to monitor the glycosylation associated with a model recombinant glycoprotein, human interferon-gamma.

Item Type: Article
DOI/Identification number: 10.1385/MB:14:3:241
Uncontrolled keywords: glycosylation; microheterogeneity; recombinant glycoproteins; oligosaccharides; capillary electrophoresis; mass spectrometry
Subjects: Q Science
Q Science > QR Microbiology
Divisions: Divisions > Division of Natural Sciences > School of Biosciences
Depositing User: O.O. Odanye
Date Deposited: 17 Apr 2009 14:29 UTC
Last Modified: 28 May 2019 13:53 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/16233 (The current URI for this page, for reference purposes)
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