Linked Life Data

1367302

Source:http://linkedlifedata.com/resource/pubmed/id/1367302

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-9-20
pubmed:abstractText
We have previously demonstrated that the expression of fully functional Fv and Fab fragments in E. coli is possible by the simultaneous secretion of both chains to the periplasm. To increase production levels and facilitate engineering and random mutagenesis, we improved our previous vectors by introducing a resident repressor gene and a filamentous phage origin. We also developed a new purification strategy based on immobilized metal ion chromatography, with which a single-chain Fv fragment can be purified to homogeneity in a single step. We investigated the most efficient tail constructions and found that only a minimal structural change of three additional C-terminal amino acids is necessary. This modification has no deleterious effect on in vivo transport and folding or antigen affinity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0733-222X
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
273-8
pubmed:dateRevised
2006-5-1
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
The functional expression of antibody Fv fragments in Escherichia coli: improved vectors and a generally applicable purification technique.
pubmed:affiliation
Genzentrum, Universität München, Max-Planck-Institut für Biochemie, Martinsried, FRG.
pubmed:publicationType
Journal Article