Abstract
The human hybridoma HB4C5 produces a lung adenocarcinoma reactive antibody (mAbC5) which possesses an unique N-linkedcarbohydrateon its light chain. We intended to design the culture environment in which the varied glycoforms on the light chain induce the alterd antigen binding affinity. HB4C5 cells were cultured in medium containing diverse carbohydrates such as monosaccharides, oligosaccharidesandpolysaccharides. Antigen bindingability ofmAbC5 significantly varied depending upon carbon sources. In particular, addition of N-acetylglucosamineandchitosan to medium led to the creation of a certain light chain glycoforms that exhibit increased antigen binding. To clarify the mechanism of carbohydratesaugement on mAbC5 light chain, the expression level of a glycogenesis-related enzyme was examined by using specific antibody. The expession level ofgalactosidasevaried depencding upon carbon sources, suggesting that the enzyme activity can be regulated by carbon sources.
Keywords
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Melchers, F. (1973) Biosynthesis, intracellular transport and secretion of immunoglobulins. Effect of 2-deoxy-D-glucose in tumor plasma cells producing and secreting immunoglobulin G1. Biochemistry, 12, 1371–1476
Yano T, Yasumoto K. Nagasima A, Hasizumi S, Murakami H and Nomoto K (1988) Immunohistological characterization of human monoclonal antibody against lung cancer. J. Surg Oncol., 39, 108–113
Hasizumi S, Kamei M, Mochizuki K, K, Sato S, Kuroda K, Kato M,, Yasumoto K, Nagahasi H, Hirose H, Tai H, Okano H, Nomoto K and Murakami H (1991) Serodiagnosis of cancer by using Candida cytochrome c recognized by human monoclonal antibody HB4C5. Hum Antibod. Hybridomas 2, 142–147
Jeremy K, Peter M.L, David A. I and Peter JD (1995) ß-1,4-Galactosyltransferase activity in B cells detected using a simple ELISA-based assay Glycobiology, 5, 365.370
Author information
Authors and Affiliations
Editor information
Rights and permissions
Copyright information
© 2002 Kluwer Academic Publishers
About this chapter
Cite this chapter
Kim, JY., Katakura, Y., Teruya, K., Shirahata, S. (2002). Modulation of Antigen Bunding of Human Antibody Via Glycosylation by Hybridoma Culture with Various Carbon Sources. In: Ikura, K., Nagao, M., Masuda, S., Sasaki, R. (eds) Animal Cell Technology: Challenges for the 21st Century. Springer, Dordrecht. https://doi.org/10.1007/0-306-46869-7_26
Download citation
DOI: https://doi.org/10.1007/0-306-46869-7_26
Publisher Name: Springer, Dordrecht
Print ISBN: 978-0-7923-5805-3
Online ISBN: 978-0-306-46869-8
eBook Packages: Springer Book Archive