| pubmed-article:9305727 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9305727 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:9305727 | lifeskim:mentions | umls-concept:C0003241 | lld:lifeskim |
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| pubmed-article:9305727 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:9305727 | lifeskim:mentions | umls-concept:C0037628 | lld:lifeskim |
| pubmed-article:9305727 | lifeskim:mentions | umls-concept:C0162801 | lld:lifeskim |
| pubmed-article:9305727 | lifeskim:mentions | umls-concept:C0033268 | lld:lifeskim |
| pubmed-article:9305727 | lifeskim:mentions | umls-concept:C0015272 | lld:lifeskim |
| pubmed-article:9305727 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:9305727 | lifeskim:mentions | umls-concept:C2700116 | lld:lifeskim |
| pubmed-article:9305727 | lifeskim:mentions | umls-concept:C0231449 | lld:lifeskim |
| pubmed-article:9305727 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:9305727 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9305727 | pubmed:dateCreated | 1997-10-15 | lld:pubmed |
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| pubmed-article:9305727 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9305727 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9305727 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9305727 | pubmed:abstractText | The cDNAs for the two variable domains of the antibody 9E10 were cloned from the hybridoma cell line. A chimeric 9E10 Fab fragment was produced in E. coli under control of the tightly controlled tetracycline promoter. The functional Fab fragment was isolated in a single step via a His6-tag, which also served for its recognition by a nickel chelate-alkaline phosphatase conjugate. Thus, the recombinant Fab fragment permitted the immunochemical detection of the myc tag in a sandwich ELISA. The dissociation constant for the interaction with the myc tag peptide was determined as 80 +/- 5 nM by fluorescence titration. In an attempt to produce the smaller 9E10 Fv fragment it was found that its V(H) domain alone can be readily isolated from E. coli as a soluble protein. This unusual behaviour may be explained by the 18 amino acid-long CDR-H3 and could be of value in the design of 'single domain' antibodies. | lld:pubmed |
| pubmed-article:9305727 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9305727 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9305727 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9305727 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9305727 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9305727 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9305727 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9305727 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:9305727 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:9305727 | pubmed:author | pubmed-author:SkerraAA | lld:pubmed |
| pubmed-article:9305727 | pubmed:author | pubmed-author:SchiweckWW | lld:pubmed |
| pubmed-article:9305727 | pubmed:author | pubmed-author:BuxbaumBB | lld:pubmed |
| pubmed-article:9305727 | pubmed:author | pubmed-author:SchätzleinCC | lld:pubmed |
| pubmed-article:9305727 | pubmed:author | pubmed-author:NeissH GHG | lld:pubmed |
| pubmed-article:9305727 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9305727 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9305727 | pubmed:volume | 414 | lld:pubmed |
| pubmed-article:9305727 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9305727 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9305727 | pubmed:pagination | 33-8 | lld:pubmed |
| pubmed-article:9305727 | pubmed:dateRevised | 2005-11-17 | lld:pubmed |
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| pubmed-article:9305727 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9305727 | pubmed:articleTitle | Sequence analysis and bacterial production of the anti-c-myc antibody 9E10: the V(H) domain has an extended CDR-H3 and exhibits unusual solubility. | lld:pubmed |
| pubmed-article:9305727 | pubmed:affiliation | Institut für Biochemie, Technische Hochschule, Darmstadt, Germany. | lld:pubmed |
| pubmed-article:9305727 | pubmed:publicationType | Journal Article | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9305727 | lld:pubmed |
