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Science 13 February 1987:
Vol. 235. no. 4790, pp. 780 - 783
DOI: 10.1126/science.2433768
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Articles

Science, Vol 235, Issue 4790, 780-783
Copyright © 1987 by American Association for the Advancement of Science

articles

Epitope mapping by chemical modification of free and antibody-bound protein antigen

A Burnens, S Demotz, G Corradin, H Binz, and HR Bosshard

A monoclonal antibody bound to a protein antigen slows the rate of chemical modification of amino acid residues located at the epitope. By comparing the degree of acetylation of 18 lysine and 7 threonine residues in free and antibody-bound horse cytochrome c, a discontiguous, conformational epitope was characterized on this protein antigen. The new approach is particularly suitable to probe discontiguous and conformational epitopes, which are difficult to analyze by other procedures.


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