| Literature DB >> 2433768 |
A Burnens, S Demotz, G Corradin, H Binz, H R Bosshard.
Abstract
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.Entities:
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Year: 1987 PMID: 2433768 DOI: 10.1126/science.2433768
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728