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Clinical Chemistry 42: 1532-1536, 1996;
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Clinical Chemistry, Vol 42, 1532-1536, Copyright © 1996 by American Association for Clinical Chemistry

Two different approaches for developing immunometric assays of haptens

J Grassi, C Creminon, Y Frobert, E Etienne, E Ezan, H Volland and P Pradelles
CEA, Service de Pharmacologie et d'Immunologie, Gif sur Yvette, France.grassi@dsvidf.cea.fr

To improve immunoassays of small haptens, we developed two different approaches for their measurement in a non-competitive format. We first devised two-site immunometric assays for small peptides (8-11 amino acids) by selecting two sets of antibodies specifically directed against C- and N-terminal moieties of the peptides. In each case, assay sensitivity improved substantially over that of the corresponding competitive assays. More interestingly, all of these new immunometric assays were much more specific than the competitive assays. In a second approach, we developed a new procedure, solid-phase-immobilized epitope immunoassay (SPIE-IA), in which a single monoclonal antibody uses the same epitope for capture and tracer binding and the hapten is covalently cross-linked to solid-phase proteins. To date, SPIE-IA have been successfully applied to the determination of haptens bearing primary amino groups, including substance P, thyroxine, leukotriene C4, endothelin, and angiotensin II. In each case, assay sensitivity was significantly improved.


The following articles in journals at HighWire Press have cited this article:


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C. Feraudet, N. Morel, S. Simon, H. Volland, Y. Frobert, C. Creminon, D. Vilette, S. Lehmann, and J. Grassi
Screening of 145 Anti-PrP Monoclonal Antibodies for Their Capacity to Inhibit PrPSc Replication in Infected Cells
J. Biol. Chem., March 25, 2005; 280(12): 11247 - 11258.
[Abstract] [Full Text] [PDF]

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 J. Biol. Chem.Home page
N. Morel, S. Simon, Y. Frobert, H. Volland, C. Mourton-Gilles, A. Negro, M. C. Sorgato, C. Creminon, and J. Grassi
Selective and Efficient Immunoprecipitation of the Disease-associated Form of the Prion Protein Can Be Mediated by Nonspecific Interactions between Monoclonal Antibodies and Scrapie-associated Fibrils
J. Biol. Chem., July 16, 2004; 279(29): 30143 - 30149.
[Abstract] [Full Text] [PDF]


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