Skip to main content
SpringerLink
Log in
Book cover

Handbook of Immunochemistry pp 309–386Cite as

Immunochemical methods

  • Chapter

Abstract

All immunochemical methods are based on a biospecific linkage between an antigen (hapten) and an antibody, or occasionally, on the non-specific interactions of free or bound antibodies with certain compounds (complement, protein A) or cell receptors (Fc-receptors). Immunochemical methods are used to demonstrate the presence of an antigen or to determine its quantity (when a specific antibody is available) or the quantity of an antibody (when a specific antigen or hapten is available). The course of the antigenantibody reaction is measured by a decrease of one of the pair of reacting components or, more frequently, by the formation of a reaction product, the antigen-antibody complex. Qualitative methods to measure immune complex formation include measurement of turbidity, precipitate, agglutinate or complement fixation. Quantitative methods make it possible to determine the amount of immune complexes produced.

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

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   39.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   54.99
Price excludes VAT (USA)
  • Compact, lightweight 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

  • Alfonso, E. (1964) Quantitative immunoelectrophoresis of serum proteins. Clin. Chim. Acta ,10, 114–22.

    Article  Google Scholar 

  • Alvine, J. C., Kemp, D. J. and Stark, G. R. (1977) Method for detection of specific RNAs in agarose gels by transfer to diazobenzyloxymethyl-paper and hybridization with DNA-probe. Proc. Natl. Acad. Sci. USA ,74, 5350–9.

    Article  Google Scholar 

  • Avrameas, S. and Uriel, J. (1966) Methode de marquege des antigens et des anticorpes avec des enzymes et son applications en immunodifusion. C. R. Acad. Sci. ,Ser. D 262, 2543–5.

    CAS  Google Scholar 

  • Bangs, L. B. (1990) New developments in particle-based tests and immunoassays. J. Int. Fed. Clin. Chem. ,2, 188–93.

    CAS  Google Scholar 

  • Beisiegel, U. (1986) Protein blotting. Electrophoresis ,7, 1–18.

    Article  CAS  Google Scholar 

  • Boitieux, J. L., Desmet, G. and Thomas, D. (1979) An “antibody electrode”, preliminary report on a new approach in enzyme immunoassay. Clin. Chem. ,25, 318–21.

    CAS  Google Scholar 

  • Burnette, W. N. (1981) “Western blotting”. electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radiolabelled protein A. Anal. Biochem. ,112, 195–204.

    Article  CAS  Google Scholar 

  • Cambiaso, C. L., Leek, A. E., de Steenwinkel, F., Billen, J. and Masson, P. L. (1977) Particle counting immunoassay (PACIA). I. A general method for the determination of antibodies, antigens and haptens. J. Immunol. Methods ,18, 33–44.

    Article  CAS  Google Scholar 

  • Carrico, R. J., Yeung, K. K., Schroeder, H. R., Boguslaski, R. C, Buckler, R. T. and Christner, J. E. (1976) Specific protein-binding reactions monitored with ligand-ATP conjugates and firefly luciferase. Anal. Biochem. ,76, 95–110.

    Article  CAS  Google Scholar 

  • Clarke, H. G. M. and Freeman, T. (1966) A quantitative immuno-electrophoresis method (Laurell electrophoresis). Protides Biol. Fluids Proc. Colloq. ,14, 503–9.

    Google Scholar 

  • Cleveland, P. H. and Richman, D. D. (1987) Enzyme immunofiltration staining assay for immediate diagnosis of herpes simplex virus and varicella-zoster virus directly from clinical specimens. J. Clin. Microbiol. ,25, 416–20.

    CAS  Google Scholar 

  • Connell, G. R., Sanders, K. M. and Williams, R. L. (1983) Electroimmunoassay. A new competitive protein-binding assay using antibody-sensitive electrodes. Biophys. J. ,44, 123–6. Coons, A. H., Creech, H. J. and Jones, R. N. (1941) Immunological properties of an antibody containing a fluorescent group. Proc. Soc. Exp. Biol. Med., 47 ,200–2.

    Article  CAS  Google Scholar 

  • Culliford, B. J. (1964) Precipitin reactions in forensic problems. Nature ,201, 1092–4.

    Article  CAS  Google Scholar 

  • Czerkinsky, C., Moldoveanu, Z., Mestecky, J., Nilsson, L.-Å. and Ouchterlony, Ö. (1988) A novel two colour ELISPOT assay. J. Immunol. Methods ,115, 31.–7.

    Article  Google Scholar 

  • Czerkinsky, C., Nilsson, L.-Å., Nygren, H., Ouchterlony, Ö. and Tarkowski, A. (1983) A solidphase enzyme-linked immunospot (ELISPOT) assay for enumeration of specific antibody-secreting cells. J. Immunol. Methods ,65, 109–21.

    Article  CAS  Google Scholar 

  • Dandliker, W. B. and Feigen, G. (1961) Quantification of the antigen-antibody reaction by the polarization of fluorescence. Biochem. Biophys. Res. Commun. ,5, 299–304.

    Article  CAS  Google Scholar 

  • Dandliker, W. B. and De Saussure, V. A. (1970) Fluorescence polarization in immunochemistry. Immunochemistry ,7, 799–828.

    Article  CAS  Google Scholar 

  • Engvall, E. and Perlmann, P. (1971) Enzyme-linked immunosorbent assay (ELISA). Quantitative assay of immunoglobulin G. Immunochemistry ,8, 871–4.

    Article  CAS  Google Scholar 

  • Fahey, J. L. and McKelvey, E. M. (1965) Quantitative determination of serum immunoglobulins in antibody-agar plates. J. Immunol. ,94, 84–91.

    CAS  Google Scholar 

  • Faulk, W. P. and Taylor, G. M. (1971) An immunocolloid method for the electron microscope. Immunochemistry ,8, 1081–3.

    Article  CAS  Google Scholar 

  • Fields, H. A., Davis, C. L., Dreesman, G. R., Bradley, D. W. and Maynard, J. E. (1981) Enzyme potentiated radioimmunoassay (EPRIA): a sensitive third-generation test for the detection of hepatitis B surface antigen. J. Immunol. Methods ,47, 145–59.

    Article  CAS  Google Scholar 

  • Gill, C. W., Fischer, C. L. and Holleman, C. L. (1971) Rapid method for protein quantitation by electroimmunodiffusion. Clin. Chem. ,17, 501–12.

    CAS  Google Scholar 

  • Gosling, J. P. (1990) A decade of development in immunoassay methodology. Clin. Chem. ,36, 1408–27.

    CAS  Google Scholar 

  • Grabar, P. and Williams, C. A. (1953) A method permitting the combined study of the electrophoretic and immunochemical properties of a mixture of proteins: application to blood serum. Biochem. Biophys. Acta ,10, 193–4.

    Article  CAS  Google Scholar 

  • Hawkes, R., Niday, E. and Gordon, J. (1982) Dot-immunobinding assay for monoclonal and other antibodies. Anal. Biochem. ,119, 142–7.

    Article  CAS  Google Scholar 

  • Hemmilä, I. (1985) Fluoroimmunoassays and immunofluorometric assays. Clin. Chem. ,31, 359–70.

    Google Scholar 

  • Henderson, D. R., Friedman, S. B., Harris, J. D., Manning, W. B. and Zaceoli, M. A. (1986) CEDIA, a new homogeneous immunoassay system. Clin. Chem. ,32, 1637–41.

    CAS  Google Scholar 

  • Jol-Van der Zijde, C. M., Labadie, J., Vlug, A., Radl, J., Vossen, J. M. and Van Tol, M. J. D. (1988) Dot-immunobinding assay as an accurate and versatile technique for the quantification of human IgG subclasses. J. Immunol. Methods ,108, 195–203.

    Article  Google Scholar 

  • Kakita, K., O’Connell, N. and Permutt, A. (1982) Immunodetection of insulin after transfer from gels to nitrocellulose filters. Diabetes ,31, 648–55.

    Article  CAS  Google Scholar 

  • Laurell, C. B. (1965) Antigen-antibody crossed electrophoresis. Anal. Biochem. ,10, 358–72.

    Article  CAS  Google Scholar 

  • Laurell, C. B. (1966) Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal. Biochem. ,15, 45–52.

    Article  CAS  Google Scholar 

  • Lauritzen, E., Masson, M., Rubin, I. and Holm, A. (1990) Dot immunobinding and immuno blotting of picogram and nanogram quantities of small peptides on activated nitrocellulose. J. Immunol. Methods ,131, 257–67.

    Article  CAS  Google Scholar 

  • Lavanchy, D., Stroun, J. and Frei, Ph. C. (1990) Modified dot assay with increased sensitivity: detection of small amounts of immunoglobulin molecules and the importance of different detection systems. J. Clin. Lab. Anal. ,4, 251–5.

    Article  CAS  Google Scholar 

  • Leute, R., Ullman, E. F. and Goldstein, A. (1972) Spin immunoassay of opiate narcotics in urine and saliva. J. Am. Med. Assoc. ,221, 1231–4.

    Article  CAS  Google Scholar 

  • Leuvering, J. H. W., Thal, P. J. H. M., Van der Waart, M. and Schuurs, A. H. W. M. (1980) Sol particle immunoassay. J. Immunoassay ,1, 77–91.

    Article  CAS  Google Scholar 

  • Mancini, G., Carbonara, A. O. and Heremans, J. F. (1965) Immunochemical quantitation of antigens by simple radial immunodiffusion. Immunochemistry ,2, 235–54.

    Article  CAS  Google Scholar 

  • Mančal, P. (1987) Methods in Enzyme Immunoassays. Prague, Institute of Sera and Vaccines, 83 pp.

    Google Scholar 

  • Mosmann, T. R. and Coffman, R. L. (1989) Thl and Th2 cells : different patterns of lymphokine secretion lead to different functional properties. Ann. Rev. Immunol. ,7, 145.

    Article  CAS  Google Scholar 

  • Nakamura, S. (1966) Cross electrophoresis: Its principles and applications. New York, Elsevier.

    Google Scholar 

  • Nakane, P. K. and Pierce, G. B. (1966) Enzyme-labelled antibodies: preparation and application for the localization of antigens. J. Histochem. Cytochem. ,14, 929–31.

    Article  CAS  Google Scholar 

  • Ouchterlony, Ö. (1948) In vitro method for testing the toxin-producing capacity of diphteria bacteria. Acta Pathol. Microbiol. Scand. ,25, 186–91.

    Article  CAS  Google Scholar 

  • Ouchterlony, Ö. (1953) Antigen-antibody reactions in gels. IV. Types of reactions in coordinated systems of diffusion. Acta Pathol. Microbiol. Scand. ,32, 231–40.

    Article  CAS  Google Scholar 

  • Oudin, J. (1956) Réaction de précipitation spécifique des sérums d’animaux de même espèce. C. R. Acad. Sci. ,242, 2489–90.

    CAS  Google Scholar 

  • Renart, J., Reiser, J. and Stark, G. R. (1979) Transfer of proteins from gels to diazobenzyl-oxymethyl-paper and detection with antisera : a method for studying antibody specificity and antigen structure. Proc. Natl. Acad. Sci. USA ,76, 3116–20.

    Article  CAS  Google Scholar 

  • Ressler, N. (1960) Two-dimensional electrophoresis of serum protein antigens in an antibody containing buffer. Clin. Chim. Acta ,5, 795–803.

    Article  CAS  Google Scholar 

  • Schroeder, H. R., Vogelhut, P. O., Carrico, R. J., Boguslaski, R. C. and Buckler, R. T. (1976) Competitive protein binding assay for biotin monitored by chemiluminescence. Anal. Chem. ,48, 1933–7.

    Article  Google Scholar 

  • Schuurs, A. H. W. M. and Van Weemen, B. K. (1977) Enzyme-immunoassay. Clin. Chim. Acta, 81, 1–40.

    Article  CAS  Google Scholar 

  • Sedgwick, J. D. and Holt, P. G. (1983) A solid-phase immunoenzymatic technique for the enumeration of specific antibody-secreting cells. J. Immunol. Methods ,57, 301–9.

    Article  CAS  Google Scholar 

  • Seitz, W. R. (1984) Immunoassay labels based on chemiluminescence and bioluminescence. Clin. Biochem. ,17, 120–5.

    Article  CAS  Google Scholar 

  • Solsky, R. L. and Rechnitz, G. A. (1981) Preparation and properties of an antibody-selective membrane electrode. Anal. Chim. Acta ,123, 135–41.

    Article  CAS  Google Scholar 

  • Southern, E. M. (1975) Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. ,98, 503–17.

    Article  CAS  Google Scholar 

  • Strasburger, C. J., Amir-Zaltsman, Y. and Kohen, F. (1988) The avidin-biotin reaction as a universal amplification system in immunoassays. In: Non-Radiometrie Assays: Technology and Application in Polypeptide and Steroid Hormone Detection. Alan R. Liss, pp. 79–100.

    Google Scholar 

  • Stryer, L. and Griffith, O. H. (1965) A spin-labelled hapten. Proc. Natl. Acad. Sci. USA ,54, 1785–91.

    Article  CAS  Google Scholar 

  • Taguchi, T., McGhee, J. R., Coffman, R. L., Beagley, K. W., Eldridge, J. H., Takatsu, K. and Kipono, H. (1990). Detection of individual mouse splenic T-cells producing IFN-γ and IL-5 using the enzyme-linked immunospot (ELISPOT) assay. J. Immunol. Methods ,128, 65–73.

    Article  CAS  Google Scholar 

  • Thompson, S. G. and Boguslaski, R. C. (1987) Homogeneous dry reagent immunoassay strips for the determination of therapeutic drugs in human serum or plasma. J. Clin. Lab. Anal., 1, 293–9.

    Article  CAS  Google Scholar 

  • Tijssen, P. (1985) Practice and Theory of Enzyme Immunoassays. Amsterdam, Elsevier Sci. Publ., 549 pp.

    Google Scholar 

  • Towbin, H., Staehelin, T. and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets : procedure and some applications. Proc. Natl. Acad. Sci. USA ,76, 4350–4.

    Article  CAS  Google Scholar 

  • Ullman, E. F., Schwarzberg, M. and Rubenstein, K. E. (1976) Fluorescence excitation transfer immunoassay. A general method for determination of antigens. J. Biol. Chem. ,251, 4172–8.

    CAS  Google Scholar 

  • Van der Sluis, P. J., Pool, C. W. and Sluiter, A. A. (1987) Press-blotting on gelatin-coated nitrocellulose membranes. A method for sensitive quantitative immunodetection of pepti-des after gel isoelectric focusing. J. Immunol. Methods ,104, 65–74.

    Article  Google Scholar 

  • Van Weemen, B. K. and Schuurs, A. H. W. M. (1971) Immunoassay using antigen-enzyme conjugate. FEBS Lett. ,15, 232–7.

    Article  Google Scholar 

  • Wilchek, M. and Bayer, E. A. (1984) The avidin-biotin complex in immunology. Immunol. Today ,5, 39–43.

    Article  CAS  Google Scholar 

  • Wilson, A. T. (1964) Direct immunoelectrophoresis. J. Immunol ,92, 431–4. Yalow, R. S. (1978) Radioimmunoassay: a probe for the fine structure of biologic systems. Science ,200, 1236–45.

    CAS  Google Scholar 

  • Yalow, R. S. and Berson, S. A. (1959) Assay of plasma insulin in human subjects by immunologi-cal methods. Nature ,184, 1648–9.

    Article  CAS  Google Scholar 

  • Zuk, R. F., Ginsberg, U. K., Houts, T., Rabbie, J., Merrick, H., Ullman, E. F., Fischer, M. M., Sizto, C. C., Stiso, S. N. and Litman, D. J. (1985) Enzyme immunochromatography -a quantitative immunoassay requiring no instrumentation. Clin. Chem. ,31, 1144–50.

    CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institute of Immunology, Faculty of Medicine, Comenius University, Bratislava, Czechoslovakia

    Miroslav Ferenčík

Authors
  1. Miroslav Ferenčík
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

Copyright information

© 1993 Springer Science+Business Media Dordrecht

About this chapter

Cite this chapter

Ferenčík, M. (1993). Immunochemical methods. In: Handbook of Immunochemistry. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-1552-0_12

Download citation

  • DOI: https://doi.org/10.1007/978-94-011-1552-0_12

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-4678-7

  • Online ISBN: 978-94-011-1552-0

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation