Effect of Environmental Parameters on Glycosylation of Recombinant Immunoglobulin G Produced from Recombinant CHO Cells-Reference-Cited by-同舟云学术

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Effect of Environmental Parameters on Glycosylation of Recombinant Immunoglobulin G Produced from Recombinant CHO Cells

Published:2018-08 Issue:4 Volume:23 Page:456-464
ISSN:1226-8372
Container-title:Biotechnology and Bioprocess Engineering
language:en
Short-container-title:Biotechnol Bioproc E

Author:

Kim Seong-Min,Chang Kyu-Ho,Oh Duk Jae

Publisher

Springer Science and Business Media LLC

Subject

Biomedical Engineering,Applied Microbiology and Biotechnology,Bioengineering,Biotechnology

Link

http://link.springer.com/content/pdf/10.1007/s12257-018-0109-8.pdf

Reference36 articles.

1. Burton, D. R. and R. A. Dwek (2006) Immunology. Sugar determines antibody activity. Scienc. 313: 670–673.

2. Raju, T. S., J. B. Briggs, S. M. Borge, and A. J. Jones (2000) Species–specific variation in glycosylation of IgG: evidence for the species–specific sialylation and branch–specific galactosylation and importance for engineering recombinant glycoprotein therapeutics. Glycobiolog. 10: 477–486.

3. Raju, T. S., J. B. Briggs, S. M. Chamow, M. E. Winkler, and A. J. Jones (2001) Glycoengineering of therapeutic glycoproteins: in vitro galactosylation and sialylation of glycoproteins with terminal N–acetylglucosamine and galactose residues. Biochemistr. 40: 8868–8876.

4. Sha, S., C. Agarabi, K. Brorson, D. Y. Lee, and S. Yoon (2016) N–Glycosylation design and control of therapeutic monoclonal antibodies. Trends Biotechnol. 34: 835–846.

5. Nimmerjahn, F., R. M. Anthony, and J. V. Ravetch (2007) Agalactosylated IgG antibodies depend on cellular Fc receptors for in vivo activity. Proc. Natl. Acad. Sci. US. 104: 8433–8437.

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