Identification of avocado (Persea americana) pulp proteins by nano-LC-MS/MS via combinatorial peptide ligand libraries.
Identifieur interne : 000227 ( Main/Exploration ); précédent : 000226; suivant : 000228Identification of avocado (Persea americana) pulp proteins by nano-LC-MS/MS via combinatorial peptide ligand libraries.
Auteurs : Clara Esteve [Espagne] ; Alfonsina D'Amato ; María Luisa Marina ; María Concepci N García ; Pier Giorgio RighettiSource :
- Electrophoresis [ 1522-2683 ] ; 2012.
Descripteurs français
- KwdFr :
- Banque de peptides (MeSH), Chromatographie en phase liquide (méthodes), Nanotechnologie (MeSH), Persea (composition chimique), Protéines végétales (analyse), Protéines végétales (classification), Protéines végétales (composition chimique), Protéome (analyse), Protéomique (MeSH), Spectrométrie de masse en tandem (méthodes), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- analyse : Protéines végétales, Protéome.
- classification : Protéines végétales.
- composition chimique : Persea, Protéines végétales.
- méthodes : Chromatographie en phase liquide, Spectrométrie de masse en tandem.
- Banque de peptides, Nanotechnologie, Protéomique, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Chromatography, Liquid (methods), Electrophoresis, Polyacrylamide Gel (MeSH), Nanotechnology (MeSH), Peptide Library (MeSH), Persea (chemistry), Plant Proteins (analysis), Plant Proteins (chemistry), Plant Proteins (classification), Proteome (analysis), Proteomics (MeSH), Tandem Mass Spectrometry (methods).
- MESH :
- chemical , analysis : Plant Proteins, Proteome.
- chemical , chemistry : Plant Proteins.
- chemical , classification : Plant Proteins.
- chemical : Peptide Library.
- chemistry : Persea.
- methods : Chromatography, Liquid, Tandem Mass Spectrometry.
- Electrophoresis, Polyacrylamide Gel, Nanotechnology, Proteomics.
Abstract
Avocado (Persea americana) proteins have been scarcely studied despite their importance, especially in food related allergies. The proteome of avocado pulp was explored in depth by extracting proteins with capture by combinatorial peptide ligand libraries at pH 7.4 and under conditions mimicking reverse-phase capture at pH 2.2. The total number of unique gene products identified amounts to 1012 proteins, of which 174 are in common with the control, untreated sample, 190 are present only in the control and 648 represent the new species detected via combinatorial peptide ligand libraries of all combined eluates and likely represent low-abundance proteins. Among the 1012 proteins, it was possible to identify the already known avocado allergen Pers a 1 and different proteins susceptible to be allergens such as a profilin, a polygalacturonase, a thaumatin-like protein, a glucanase, and an isoflavone reductase like protein.
DOI: 10.1002/elps.201200254
PubMed: 23019098
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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first="María Luisa" last="Marina">María Luisa Marina</name></author><author><name sortKey="Garcia, Maria Concepci N" sort="Garcia, Maria Concepci N" uniqKey="Garcia M" first="María Concepci N" last="García">María Concepci N García</name></author><author><name sortKey="Righetti, Pier Giorgio" sort="Righetti, Pier Giorgio" uniqKey="Righetti P" first="Pier Giorgio" last="Righetti">Pier Giorgio Righetti</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:23019098</idno><idno type="pmid">23019098</idno><idno type="doi">10.1002/elps.201200254</idno><idno type="wicri:Area/Main/Corpus">000211</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000211</idno><idno type="wicri:Area/Main/Curation">000211</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000211</idno><idno 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sort="Marina, Maria Luisa" uniqKey="Marina M" first="María Luisa" last="Marina">María Luisa Marina</name></author><author><name sortKey="Garcia, Maria Concepci N" sort="Garcia, Maria Concepci N" uniqKey="Garcia M" first="María Concepci N" last="García">María Concepci N García</name></author><author><name sortKey="Righetti, Pier Giorgio" sort="Righetti, Pier Giorgio" uniqKey="Righetti P" first="Pier Giorgio" last="Righetti">Pier Giorgio Righetti</name></author></analytic><series><title level="j">Electrophoresis</title><idno type="eISSN">1522-2683</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chromatography, Liquid (methods)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Nanotechnology (MeSH)</term><term>Peptide Library (MeSH)</term><term>Persea (chemistry)</term><term>Plant Proteins (analysis)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (classification)</term><term>Proteome (analysis)</term><term>Proteomics (MeSH)</term><term>Tandem Mass Spectrometry (methods)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Banque de peptides (MeSH)</term><term>Chromatographie en phase liquide (méthodes)</term><term>Nanotechnologie (MeSH)</term><term>Persea (composition chimique)</term><term>Protéines végétales (analyse)</term><term>Protéines végétales (classification)</term><term>Protéines végétales (composition chimique)</term><term>Protéome (analyse)</term><term>Protéomique (MeSH)</term><term>Spectrométrie de masse en tandem (méthodes)</term><term>Électrophorèse sur gel de polyacrylamide (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Plant Proteins</term><term>Proteome</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="classification" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Peptide Library</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Protéines végétales</term><term>Protéome</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Persea</term></keywords><keywords scheme="MESH" qualifier="classification" xml:lang="fr"><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Persea</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Chromatography, Liquid</term><term>Tandem Mass Spectrometry</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Chromatographie en phase liquide</term><term>Spectrométrie de masse en tandem</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electrophoresis, Polyacrylamide Gel</term><term>Nanotechnology</term><term>Proteomics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Banque de peptides</term><term>Nanotechnologie</term><term>Protéomique</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Avocado (Persea americana) proteins have been scarcely studied despite their importance, especially in food related allergies. The proteome of avocado pulp was explored in depth by extracting proteins with capture by combinatorial peptide ligand libraries at pH 7.4 and under conditions mimicking reverse-phase capture at pH 2.2. The total number of unique gene products identified amounts to 1012 proteins, of which 174 are in common with the control, untreated sample, 190 are present only in the control and 648 represent the new species detected via combinatorial peptide ligand libraries of all combined eluates and likely represent low-abundance proteins. Among the 1012 proteins, it was possible to identify the already known avocado allergen Pers a 1 and different proteins susceptible to be allergens such as a profilin, a polygalacturonase, a thaumatin-like protein, a glucanase, and an isoflavone reductase like protein.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23019098</PMID><DateCompleted><Year>2013</Year><Month>01</Month><Day>29</Day></DateCompleted><DateRevised><Year>2012</Year><Month>09</Month><Day>28</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1522-2683</ISSN><JournalIssue CitedMedium="Internet"><Volume>33</Volume><Issue>18</Issue><PubDate><Year>2012</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Electrophoresis</Title><ISOAbbreviation>Electrophoresis</ISOAbbreviation></Journal><ArticleTitle>Identification of avocado (Persea americana) pulp proteins by nano-LC-MS/MS via combinatorial peptide ligand libraries.</ArticleTitle><Pagination><MedlinePgn>2799-805</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/elps.201200254</ELocationID><Abstract><AbstractText>Avocado (Persea americana) proteins have been scarcely studied despite their importance, especially in food related allergies. The proteome of avocado pulp was explored in depth by extracting proteins with capture by combinatorial peptide ligand libraries at pH 7.4 and under conditions mimicking reverse-phase capture at pH 2.2. The total number of unique gene products identified amounts to 1012 proteins, of which 174 are in common with the control, untreated sample, 190 are present only in the control and 648 represent the new species detected via combinatorial peptide ligand libraries of all combined eluates and likely represent low-abundance proteins. Among the 1012 proteins, it was possible to identify the already known avocado allergen Pers a 1 and different proteins susceptible to be allergens such as a profilin, a polygalacturonase, a thaumatin-like protein, a glucanase, and an isoflavone reductase like protein.</AbstractText><CopyrightInformation>© 2012 WILEY-VCH Verlag GmbH & Co. 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