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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1991-10-28
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X58641,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X58642,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X58643,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X58644,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X58645,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X58646,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X58647,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X58648,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X58649,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X58650
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pubmed:abstractText |
We describe three sets of natural (preimmune) polyreactive antibodies and Ag-induced antibodies that share the same VH-VL combinations. The amino acid homology in the VH and VL segments averaged 92%. These sets were found among 49 neonatal and adult natural mAb that were compared with 35 Ag-induced monoclonals produced during the memory response to phosphocholine (PC)-keyhole limpet hemocyanin. Both groups of monoclonals had been selected on the basis of a restricted fine specificity pattern, namely the ability to recognize PC-protein and p-nitrophenyl phosphocholine but not PC. All of the antibodies were tested for reactivity against a panel of 15 self and foreign Ag. Despite their common fine specificity as the basis for selection, 33/49 natural antibodies were poly/auto reactive whereas 0/35 Ag-induced antibodies had such poly/auto reactive properties. The natural antibodies were encoded by genes representing nine different VH families and several V kappa and V lambda families. There were a few replacement substitutions distinguishing the Ag-induced antibodies from the natural antibodies in each set; however, the most noteworthy difference was the extreme variability of CDR3 in the natural antibodies that differed in both length and amino acid sequence from each other and from Ag-induced antibodies. The results suggest that CDR3 of the H chain may play a critical role in distinguishing poly- from monospecific combining sites in natural and Ag-induced antibodies.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
|
pubmed:volume |
147
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
2359-67
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1918968-Amino Acid Sequence,
pubmed-meshheading:1918968-Animals,
pubmed-meshheading:1918968-Antibodies,
pubmed-meshheading:1918968-Base Sequence,
pubmed-meshheading:1918968-Genes, Immunoglobulin,
pubmed-meshheading:1918968-Hybridomas,
pubmed-meshheading:1918968-Immunoglobulin Heavy Chains,
pubmed-meshheading:1918968-Immunoglobulin Variable Region,
pubmed-meshheading:1918968-Mice,
pubmed-meshheading:1918968-Mice, Inbred BALB C,
pubmed-meshheading:1918968-Molecular Sequence Data,
pubmed-meshheading:1918968-Phenotype
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pubmed:year |
1991
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pubmed:articleTitle |
Natural auto- and polyreactive antibodies differing from antigen-induced antibodies in the H chain CDR3.
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pubmed:affiliation |
Department of Microbiology and Immunology, Oregon Health Sciences University, Portland 97201.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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