rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
6
|
pubmed:dateCreated |
2005-12-12
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pubmed:abstractText |
A problem faced in proteomics studies is the recovery of tagged protein complexes in their native and active form. Here we describe a peptide, Bio-Ox, that mimics the immunoglobulin G (IgG) binding interface of Staphylococcus aureus Protein A, and competitively displaces affinity-purified Protein A fusion proteins and protein complexes from IgG-Sepharose. We show that Bio-Ox elution is a robust method for the efficient and rapid recovery of native tagged proteins, and can be applied to a variety of structural genomics and proteomics studies.
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pubmed:grant |
|
pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:issn |
1535-3893
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
4
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2250-6
|
pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16335973-Bacterial Proteins,
pubmed-meshheading:16335973-Biochemistry,
pubmed-meshheading:16335973-Biotin,
pubmed-meshheading:16335973-Chromatography, Affinity,
pubmed-meshheading:16335973-Hydrogen-Ion Concentration,
pubmed-meshheading:16335973-Immunoglobulin G,
pubmed-meshheading:16335973-Models, Chemical,
pubmed-meshheading:16335973-Peptides,
pubmed-meshheading:16335973-Proteins,
pubmed-meshheading:16335973-Proteomics,
pubmed-meshheading:16335973-Recombinant Fusion Proteins,
pubmed-meshheading:16335973-Sepharose,
pubmed-meshheading:16335973-Staphylococcus aureus,
pubmed-meshheading:16335973-Temperature,
pubmed-meshheading:16335973-Time Factors
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pubmed:articleTitle |
A method for the rapid and efficient elution of native affinity-purified protein A tagged complexes.
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pubmed:affiliation |
Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, NY 10021-6399, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|