pubmed-article:9836471 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9836471 | lifeskim:mentions | umls-concept:C0004651 | lld:lifeskim |
pubmed-article:9836471 | lifeskim:mentions | umls-concept:C0027651 | lld:lifeskim |
pubmed-article:9836471 | lifeskim:mentions | umls-concept:C0221908 | lld:lifeskim |
pubmed-article:9836471 | lifeskim:mentions | umls-concept:C0003241 | lld:lifeskim |
pubmed-article:9836471 | lifeskim:mentions | umls-concept:C0005516 | lld:lifeskim |
pubmed-article:9836471 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
pubmed-article:9836471 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:9836471 | pubmed:dateCreated | 1998-12-7 | lld:pubmed |
pubmed-article:9836471 | pubmed:abstractText | The tumour-associated antigen epithelial glycoprotein-2 (EGP-2) is a promising target for detection and treatment of a variety of human carcinomas. Antibodies to this antigen have been successfully used in patients for imaging of small-cell lung cancer and for adjuvant treatment of minimal residual disease of colon cancer. We describe here the isolation and complete characterization of high-affinity single-chain variable fragments (scFv) to the EGP-2 antigen. First, the binding kinetics of four murine whole antibodies directed to EGP-2 (17-1A, 323/A3, MOC-31 and MOC-161) were determined using surface plasmon resonance (SPR). The MOC-31 antibody has the lowest apparent off-rate, followed by MOC-161 and 323/A3. The V-genes of the two MOC hybridomas were cloned as scFv in a phage display vector and antigen-binding phage were selected by panning on recombinant antigen. The scFvs compete with the original hybridoma antibodies for binding to antigen and specifically bind to human carcinomas in immunohistochemistry. MOC-31 scFv has an off-rate which is better than those of the bivalent 17-1A and 323/A3 whole antibodies, providing it with an essential characteristic for tumour retention in vivo. The availability of these high-affinity anti-EGP-2 antibody fragments and of their encoding V-genes creates a variety of possibilities for their future use as tumour-targeting vehicles. | lld:pubmed |
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pubmed-article:9836471 | pubmed:language | eng | lld:pubmed |
pubmed-article:9836471 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9836471 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9836471 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9836471 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9836471 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9836471 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9836471 | pubmed:month | Dec | lld:pubmed |
pubmed-article:9836471 | pubmed:issn | 0007-0920 | lld:pubmed |
pubmed-article:9836471 | pubmed:author | pubmed-author:HelfrichWW | lld:pubmed |
pubmed-article:9836471 | pubmed:author | pubmed-author:de LeijLL | lld:pubmed |
pubmed-article:9836471 | pubmed:author | pubmed-author:HenderikxPP | lld:pubmed |
pubmed-article:9836471 | pubmed:author | pubmed-author:HoogenboomH... | lld:pubmed |
pubmed-article:9836471 | pubmed:author | pubmed-author:de BruïneA... | lld:pubmed |
pubmed-article:9836471 | pubmed:author | pubmed-author:ArendsJ WJW | lld:pubmed |
pubmed-article:9836471 | pubmed:author | pubmed-author:van der... | lld:pubmed |
pubmed-article:9836471 | pubmed:author | pubmed-author:RooversR CRC | lld:pubmed |
pubmed-article:9836471 | pubmed:author | pubmed-author:ReursAA | lld:pubmed |
pubmed-article:9836471 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9836471 | pubmed:volume | 78 | lld:pubmed |
pubmed-article:9836471 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9836471 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9836471 | pubmed:pagination | 1407-16 | lld:pubmed |
pubmed-article:9836471 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:9836471 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9836471 | pubmed:articleTitle | High-affinity recombinant phage antibodies to the pan-carcinoma marker epithelial glycoprotein-2 for tumour targeting. | lld:pubmed |
pubmed-article:9836471 | pubmed:affiliation | Department of Pathology, Maastricht University, The Netherlands. | lld:pubmed |
pubmed-article:9836471 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9836471 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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