Epitope mapping by chemical modification of free and antibody-bound protein antigen
Détails
ID Serval
serval:BIB_FCD51A980DB9
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Epitope mapping by chemical modification of free and antibody-bound protein antigen
Périodique
Science
ISSN
0036-8075 (Print)
Statut éditorial
Publié
Date de publication
02/1987
Volume
235
Numéro
4790
Pages
780-3
Notes
Comparative Study
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Feb 13
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Feb 13
Résumé
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.
Mots-clé
Amino Acid Sequence
Animals
Antibodies, Monoclonal/*immunology
*Antigen-Antibody Complex
Cytochrome c Group/*immunology
Epitopes/*immunology
Horses
Humans
Models, Molecular
Protein Conformation
Species Specificity
Pubmed
Web of science
Création de la notice
24/01/2008 15:55
Dernière modification de la notice
20/08/2019 17:27