Linked Life Data

7764430

Source:http://linkedlifedata.com/resource/pubmed/id/7764430

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-3-31
pubmed:abstractText
As a model system for the optimization of separation ligands by bacteriophage surface display, we have constructed a phage surface expression system for a single immunoglobulin-binding domain of Protein A of Staphylococcus aureus. Protein A domain B is genetically fused to the gpIII adsorption protein of the filamentous bacteriophage M13, and hence displayed on the phage surface. Phage displaying the Protein A domain are selectively retained on human IgG-sepharose. Retention is due to specific Protein A-IgG interactions, as demonstrated by competitive inhibition by soluble Protein A or polyclonal human IgG. Polyclonal goat IgG, which is known to bind less well to Protein A than does human IgG, inhibits phage adsorption less effectively. Phage expressing Protein A can be purified in a few rounds of selective adsorption from a vast excess of wild type phage. Diverse libraries constructed by mutagenesis of this construct will allow massive screening of mutant forms of Protein A for alterations in binding and elution properties. We anticipate that phage display will prove to be a widely-applicable method of identification and optimization of affinity ligands for separations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0733-222X
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
169-72
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Bacteriophage surface display of an immunoglobulin-binding domain of Staphylococcus aureus protein A.
pubmed:affiliation
Department of Biochemical and Biophysical Sciences, University of Houston, Texas 77204.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't