Skip to main content

Ranking the Affinities of Monoclonal Antibodies

  • Chapter

Part of the book series: Contemporary Biomedicine ((CB,volume 7))

Abstract

A set of monoclonal antibodies to an antigen can be prepared for many different reasons, such as structural investigation, purification by immunoabsorption, immunoassay, or immunohistochemistry. For these purposes, different properties of the antibodies are useful, and the number of different antibodies likely to be available after a single fusion makes possible rational selection of each particular monoclonal antibody in a way that was never possible when polyclonal antisera were all that were available.

This is a preview of subscription content, log in via an institution.

Buying options

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   169.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   219.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD   219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Froese A.: 1968. Kinetic and equilibrium studies on 2,4-dinitrophenyl hapten-antibody systems. Immunochemistry 5: 253–264.

    Article  PubMed  CAS  Google Scholar 

  2. Karush F.: 1978. The affinity of antibody: range, variability, and the role of multivalence. Compr. Immunol. 5: 85–116.

    CAS  Google Scholar 

  3. van Heyningen V., Brock D. J. H., and van Heyningen S.: 1983. A simple method for ranking the affinities of monoclonal antibodies. J. Immunol. Meth. 62: 147–153.

    Article  Google Scholar 

  4. Scatchard G.: 1949. The attraction of proteins for small molecules and ions. Ann. NY Acad. Sci. 51: 660–672.

    Article  CAS  Google Scholar 

  5. Klotz I. M.: 1982. Numbers of receptor sites from Scatchard graphs: facts and fantasies. Science 217: 1247–1249.

    Article  PubMed  CAS  Google Scholar 

  6. Adrion R. F.: 1982. Immunoassay design equation. Clin. Chem. 28: 717.

    PubMed  CAS  Google Scholar 

  7. Springer T. A.: 1983. Quantitation of hybridoma immunoglobulins and selection of light-chain loss variants. Meth. Enzymol. 92: 147–160.

    Article  PubMed  CAS  Google Scholar 

  8. van Heyningen V., Barron L., Brock D. J. H., Crichton D., and Lawrie S.: 1982. Monoclonal antibodies to human alphafetoprotein: analysis of the behavior of three different antibodies. J. Immunol. Meth. 50: 123–132.

    Article  Google Scholar 

  9. Seth J., Kellet H. A., Caldwell G., Sweeting V. M., Becket G. J., Gow S. M., and Toft A. D.: 1984. A sensitive immunoradiometric assay for serum thyroid stimulating hormone: a replacement for the thyrotrophin releasing hormone test? Brit. Med. J. 289: 1334–1336.

    Article  CAS  Google Scholar 

Download references

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1987 The Humana Press Inc.

About this chapter

Cite this chapter

van Heyningen, V., van Heyningen, S. (1987). Ranking the Affinities of Monoclonal Antibodies. In: Bartal, A.H., Hirshaut, Y. (eds) Methods of Hybridoma Formation. Contemporary Biomedicine, vol 7. Humana Press. https://doi.org/10.1007/978-1-4612-4826-2_20

Download citation

  • DOI: https://doi.org/10.1007/978-1-4612-4826-2_20

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-4612-9179-4

  • Online ISBN: 978-1-4612-4826-2

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics