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The Analysis of Antigen-Antibody Binding Using Anti-RNase A Single Chain Fv-3A21

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Abstract

In this study, the effect of amino acid residues on antigen-antibody binding was investigated. The cDNA of the V region of antibody 3A21 was cloned using PCR method. From sequence data, compared with other residues, higher numbers of aspartate and glutamate residues existed in the binding region of antibody 3A21. It suggested that the electrostatic bound had an important role in antigen-antibody binding. In order to investigate the role of the amino acid residues of the binding site, the single chain Fv was constructed and expressed as a phage antibody. The affinity constant of the single chain Fv-3A21 was almost the same as that of native antibody 3A21.

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References

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T. Kobayashi Y. Kitagawa K. Okumura

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© 1994 Springer Science+Business Media Dordrecht

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Kobayashi, E., Kumamoto, T., Omasa, T., Fujiyama, K., Shioya, S., Suga, Ki. (1994). The Analysis of Antigen-Antibody Binding Using Anti-RNase A Single Chain Fv-3A21. In: Kobayashi, T., Kitagawa, Y., Okumura, K. (eds) Animal Cell Technology: Basic & Applied Aspects. The Sixth International Meeting of Japanese Association for Animal Cell Technology JAACT’93, vol 6. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-0848-5_36

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  • DOI: https://doi.org/10.1007/978-94-011-0848-5_36

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-4366-3

  • Online ISBN: 978-94-011-0848-5

  • eBook Packages: Springer Book Archive

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