Linked Life Data

8111478

Source:http://linkedlifedata.com/resource/pubmed/id/8111478

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-3-30
pubmed:abstractText
A procedure was developed for the rapid isolation of an antibody Fv fragment expressed in Escherichia coli via immobilized metal affinity chromatography. Metal affinity was mediated by fusing hexahistidine tails to both the VL and the VH domain and was thus independent of the antigen-binding specificity. Unexpectedly, it was not possible to isolate the Fv fragment with correct stoichiometric composition of the two variable domains under standard chromatographic conditions. Proper non-covalent association of VL and VH was, however, maintained when using glycine betaine as electrolyte, thus permitting purification of the intact Fv fragment to homogeneity in a single step.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9673
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
657
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
55-61
pubmed:dateRevised
2009-1-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Single-step purification of a bacterially expressed antibody Fv fragment by immobilized metal affinity chromatography in the presence of betaine.
pubmed:affiliation
Max-Planck-Institut für Biophysik, Abt. Molekulare Membranbiologie, Frankfurt/Main, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't