Source:http://linkedlifedata.com/resource/pubmed/id/20723137
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2011-5-6
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pubmed:abstractText |
The major challenge of follicular fluid proteomic analysis is the presence of high-abundance proteins that originate from plasma. These proteins can prevent the detection of lower abundant ones, produced locally by follicle cells and that may have important roles in follicular activity. In this study, the novel technology called hexapeptide ligand library was evaluated to enrich the low-abundance proteins in follicular fluid of human (HFF), porcine (PFF) and equine (EFF) prior 2D-PAGE. Our results showed that the new strategy enabled detection of many new protein spots, increased resolution and highly improved the intensity of low-abundance proteins by 2D-PAGE.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1439-0531
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pubmed:author | |
pubmed:copyrightInfo |
© 2010 Blackwell Verlag GmbH.
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pubmed:issnType |
Electronic
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pubmed:volume |
46
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
561-3
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pubmed:meshHeading |
pubmed-meshheading:20723137-Animals,
pubmed-meshheading:20723137-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:20723137-Female,
pubmed-meshheading:20723137-Follicular Fluid,
pubmed-meshheading:20723137-Horses,
pubmed-meshheading:20723137-Humans,
pubmed-meshheading:20723137-Peptide Library,
pubmed-meshheading:20723137-Proteins,
pubmed-meshheading:20723137-Proteomics,
pubmed-meshheading:20723137-Swine
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pubmed:year |
2011
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pubmed:articleTitle |
Improvement of 2D-PAGE resolution of human, porcine and equine follicular fluid by means of hexapeptide ligand library.
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pubmed:affiliation |
Physiologie de la Reproduction et des Comportements, Nouzilly, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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