Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
|
pubmed:dateCreated |
1990-7-18
|
pubmed:abstractText |
Four anti-idiotopic mAB, 107, MB, AI, and AD8, react with mouse hybridoma protein 36-65 specific for the hapten p-azophenylarsonate. The four antiidiotypic antibodies do not react with hybridoma protein 36-71, a somatically mutated variant of 36-65 whose H and L chain V region sequence differs at 19 amino acid positions. To determine which regions of 36-65 are important for the interaction with each of the four anti-idiotypic antibodies, variants of 36-65 containing one or more of the 36-71 substitutions were generated by oligonucleotide-directed mutagenesis of the rearranged 36-65 H chain V region gene, followed by expression of mutant proteins containing either the 36-65 or the 36-71 L chain in transfected hybridoma cells. Idiotypic characterization of the mutant proteins showed that reactivity correlates with the 36-65 H chain, but some contributions from the 36-65 L chain come into play. In the 36-65 H chain V region, idiotopes were mapped to the first and third complementarity-determining regions for anti-idiotypic antibodies 107, MB, and AI, and to all three complementarity-determining regions for anti-idiotypic antibody AD8. The binding of all four anti-idiotypic antibodies to hybridoma protein 36-65 was hapten inhibitable. However, a comparison between the effect of individual 36-71 substitutions on idiotope expression and their effect on Ag-binding affinity suggests that none of the four anti-idiotypic antibodies bodies mimics the structure of Ag.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
AIM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Anti-Idiotypic,
http://linkedlifedata.com/resource/pubmed/chemical/Haptens,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Idiotypes,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotides
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0022-1767
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
144
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
4863-9
|
pubmed:dateRevised |
2011-11-17
|
pubmed:meshHeading |
pubmed-meshheading:2351832-Amino Acid Sequence,
pubmed-meshheading:2351832-Animals,
pubmed-meshheading:2351832-Antibodies, Anti-Idiotypic,
pubmed-meshheading:2351832-Base Sequence,
pubmed-meshheading:2351832-Binding Sites, Antibody,
pubmed-meshheading:2351832-DNA Mutational Analysis,
pubmed-meshheading:2351832-Haptens,
pubmed-meshheading:2351832-Immunoglobulin G,
pubmed-meshheading:2351832-Immunoglobulin Idiotypes,
pubmed-meshheading:2351832-Mice,
pubmed-meshheading:2351832-Molecular Sequence Data,
pubmed-meshheading:2351832-Oligonucleotides
|
pubmed:year |
1990
|
pubmed:articleTitle |
Structural characterization of idiotopes by using antibody variants generated by site-directed mutagenesis.
|
pubmed:affiliation |
Department of Pathology, Hubert H. Humphrey Cancer Research Center, Boston University School of Medicine, MA 02118.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|