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Clinical Chemistry and Laboratory Medicine (CCLM)

Published in Association with the European Federation of Clinical Chemistry and Laboratory Medicine (EFLM)

Editor-in-Chief: Plebani, Mario

Ed. by Gillery, Philippe / Lackner, Karl J. / Lippi, Giuseppe / Melichar, Bohuslav / Payne, Deborah A. / Schlattmann, Peter / Tate, Jillian R.

12 Issues per year


IMPACT FACTOR 2016: 3.432

CiteScore 2016: 2.21

SCImago Journal Rank (SJR) 2016: 1.000
Source Normalized Impact per Paper (SNIP) 2016: 1.112

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ISSN
1437-4331
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Volume 38, Issue 3

Issues

Quality Control of Coated Antibodies: New, Rapid Determination of Binding Affinity

Rémy Ricoux / Bénédicte Chazaud / Jean-Pierre Tresca / Michel Pontet
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/CCLM.2000.035

Abstract

A procedure is described for the determination of the affinity constant between a fluid-phase biotinylated antigen and a solid-phase monoclonal antibody. This procedure allows evaluation of the efficiency of an antibody as a coated tool for an immunoassay. For this purpose, the biotinylation of the antigen and its further quantitative measurement by streptavidin-peroxidase led to a single reversible interaction, the binding affinity of which greatly determines the quality of the assay. The free and bound fractions of the biotinylated antigen were obtained in wells coated with a low level of immobilized antibodies. At the equilibrium state, the free antigen present in the supernatant of these wells was further transferred to high level antibody coated wells which captured all the free antigen molecules. These molecules were quantified using a standard curve established with known concentrations of biotinylated antigen, also incubated in wells coated with the high level of antibody.

About the article

Published Online: 2005-06-01

Published in Print: 2000-03-25


Citation Information: Clinical Chemistry and Laboratory Medicine, Volume 38, Issue 3, Pages 239–243, ISSN (Print) 1434-6621, DOI: https://doi.org/10.1515/CCLM.2000.035.

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