Strutton, B., Jaffé, S.R.P., Pandhal, J. et al. (1 more author) (2017) Generation of Recombinant N-Linked Glycoproteins in E. coli. In: Burgess-Brown, N.A., (ed.) Heterologous Gene Expression in E.coli. Methods in Molecular Biology, 1586 (1586). Springer New York , pp. 233-250.
Abstract
The production of N-linked recombinant glycoproteins is possible in a variety of biotechnology host cells, and more recently in the bacterial workhorse, Escherichia coli. This methods chapter will outline the components and procedures needed to produce N-linked glycoproteins in E. coli, utilizing Campylobacter jejuni glycosylation machinery, although other related genes can be used with minimal tweaks to this methodology. To ensure a successful outcome, various methods will be highlighted that can confirm glycoprotein production to a high degree of confidence, including the gold standard of mass spectrometry analysis.
Metadata
Item Type: | Book Section |
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Authors/Creators: |
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Editors: |
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Copyright, Publisher and Additional Information: | © 2017 Springer. This is an author produced version of a paper subsequently published in Heterologous Gene Expression in E.coli. Uploaded in accordance with the publisher's self-archiving policy.The final publication is available at Springer via http://dx.doi.org/10.1007/978-1-4939-6887-9_15. |
Keywords: | Glycosylation; N-Linked glycoproteins; Posttranslational modifications; E. coli; Glycoprotein validation |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Engineering (Sheffield) > Department of Chemical and Biological Engineering (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 23 Jun 2017 09:48 |
Last Modified: | 04 May 2018 00:38 |
Published Version: | https://doi.org/10.1007/978-1-4939-6887-9_15 |
Status: | Published |
Publisher: | Springer New York |
Series Name: | Methods in Molecular Biology |
Refereed: | Yes |
Identification Number: | 10.1007/978-1-4939-6887-9_15 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:117794 |