Publication Date:
1987-02-13
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burnens, A -- Demotz, S -- Corradin, G -- Binz, H -- Bosshard, H R -- New York, N.Y. -- Science. 1987 Feb 13;235(4790):780-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2433768" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Antibodies, Monoclonal/*immunology
;
*Antigen-Antibody Complex
;
Cytochrome c Group/*immunology
;
Epitopes/*immunology
;
Horses
;
Humans
;
Models, Molecular
;
Protein Conformation
;
Species Specificity
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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