Methods for measurement of antibody/antigen affinity based on ELISA and RIA

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department
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whocc
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Administrative Staff
Assistant Professor
Associate Professor
Clinical Research Assistant
Clinical Research Nurse
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Dual-education Student
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Lab assistant
Master Student
Non-permanent Researcher
Nursing Staff
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Pharmacist
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Research Associate
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Visiting Scientist

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Deputy Director of Department
Deputy Director of National Reference Center
Deputy Head of Facility
Director of Center
Director of Department
Director of Institute
Director of National Reference Center
Group Leader
Head of Facility
Head of Operations
Head of Structure
Honorary President of the Departement
Labex Coordinator

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Nicking of the tryptophan synthase beta 2-subunit at Glu-296 prevents the conformational change undergone on binding the alpha-subunit

Crystallization and preliminary crystallographic analysis of a tetrameric isolectin from Vicia villosa, specific for the Tn antigen

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Diseases

Organisms

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Technique

Published in Current opinion in immunology - 01 Apr 1993

Goldberg ME, Djavadi-Ohaniance L

Link to Pubmed [PMID] – 8507406

Curr. Opin. Immunol. 1993 Apr;5(2):278-81

Various enzyme-linked immunosorbent assay or radioimmunoassay methods are currently used to quantify the antibody-antigen interaction. Only those based on indirect competition–enzyme-linked immunosorbent assay or radioimmunoassay–can provide the real thermodynamic affinity of the antibody for its antigen. They can be applied to a variety of experimental situations, some of which are reviewed here.

Published on: 01 Apr 1993