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Screening of monoclonal antibodies using antigens labeled with acetylcholinesterase: Application to the peripheral proteins of photosystem 1 by Jacques Grassi; Yveline Frobert; Patricia Lamourette; Bernard Lagoutte is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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An original immunoenzymatic screening method, based on the use of antigens labeled with the stable enzyme acetylcholinesterase (AChE, EC 3.1.1.7), is described. The high turnover of this enzyme results in a very sensitive detection of antibodies. In this method, monoclonal antibodies from the supernatants of hybridoma cultures are immobilized on a solid phase coated with anti-mouse immunoglobulins and react simultaneously with the appropriate antigen labeled with biotin molecules. In a second step, biotinylated acetylcholinesterase is in turn associated to the system via avidin interactions and subsequently detected by a colorimetric assay. The method appears more sensitive and easier to use than either the corresponding radioimmunological test using a 125I-iodinated antigen or the same type of enzymatic immunoassay performed with biotinylated horseradish peroxidase instead of biotinylated AChE. The combined use of microtiter plates, solid-phase separation, and colorimetric detection allows a high level of automation of the method which makes it very efficient to process a large number of samples. This technique has been successfully applied to the screening of monoclonal antibodie

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Author

Jacques Grassi; Yveline Frobert; Patricia Lamourette; Bernard Lagoutte

Publisher

Elsevier Science; Elsevier ; Elsevier Inc.; Elsevier BV (ISSN 0003-2697)

Published

1988

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)