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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4790
|
| pubmed:dateCreated |
1987-3-11
|
| pubmed:abstractText |
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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0036-8075
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
13
|
| pubmed:volume |
235
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
780-3
|
| pubmed:dateRevised |
2007-3-19
|
| pubmed:meshHeading |
pubmed-meshheading:2433768-Amino Acid Sequence,
pubmed-meshheading:2433768-Animals,
pubmed-meshheading:2433768-Antibodies, Monoclonal,
pubmed-meshheading:2433768-Antigen-Antibody Complex,
pubmed-meshheading:2433768-Cytochrome c Group,
pubmed-meshheading:2433768-Epitopes,
pubmed-meshheading:2433768-Horses,
pubmed-meshheading:2433768-Humans,
pubmed-meshheading:2433768-Models, Molecular,
pubmed-meshheading:2433768-Protein Conformation,
pubmed-meshheading:2433768-Species Specificity
|
| pubmed:year |
1987
|
| pubmed:articleTitle |
Epitope mapping by chemical modification of free and antibody-bound protein antigen.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|