AI Article Synopsis
- The study investigated the epitope structure of human alpha-fetoprotein (AFP) using over 50 monoclonal antibodies from international workshops.
- Researchers analyzed the AFP-antibody interactions through competitive immunoaffinity electrochromatography on nitrocellulose membranes, identifying five types of interactions including complete and partial neutralization.
- The findings led to the creation of an epitope map for AFP, highlighting 23 distinct epitopes and discussing the implications of these interactions on the AFP molecule's structure.
Article Abstract
The epitope structure of human alpha-fetoprotein (AFP) was studied using more than 50 monoclonal antibodies (MAB) to human AFP. These MAB obtained from various world laboratories of the TD-2 AFP Workshops of the International Society for Oncodevelopmental Biology and Medicine (ISOBM-1996-1998-2000) were analyzed by competitive immunoaffinity electrochromatography (IAE) on nitrocellulose membranes (NCM). Five types of interaction of the AFP-MAB complex with the MAB fixed on NCM were found: 1) complete neutralization; 2) partial neutralization; 3) unidirectional neutralization; 4) enhanced binding; 5) lack of interaction. By IAE, 51 MAB were found to recognize 23 different epitopes in the AFP molecule. Based on these findings, an epitope map of AFP was designed which consists of eight epitope clusters and eight individual epitopes. The epitope location is considered with respect to the conformational state of the AFP molecule. Possible causes of the five types of interaction found on neutralization are discussed.
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| http://dx.doi.org/10.1023/a:1010258902421 | DOI Listing |
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