Development of an enrichment method for endogenous phosphopeptide characterization in human serum
The work describes the development of an enrichment method for the analysis of endogenous phosphopeptides in serum. Endogenous peptides can play significant biological roles, and some of them could be exploited as future biomarkers. In this context, blood is one of the most useful biofluids for scre...
Gespeichert in:
| Veröffentlicht in: | Analytical and bioanalytical chemistry 2018-01, Vol.410 (3), p.1177-1185 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1185 |
|---|---|
| container_issue | 3 |
| container_start_page | 1177 |
| container_title | Analytical and bioanalytical chemistry |
| container_volume | 410 |
| creator | La Barbera, Giorgia Capriotti, Anna Laura Cavaliere, Chiara Ferraris, Francesca Laus, Michele Piovesana, Susy Sparnacci, Katia Laganà, Aldo |
| description | The work describes the development of an enrichment method for the analysis of endogenous phosphopeptides in serum. Endogenous peptides can play significant biological roles, and some of them could be exploited as future biomarkers. In this context, blood is one of the most useful biofluids for screening, but a systematic investigation of the endogenous peptides, especially phosphorylated ones, is still lacking, mainly due to the lack of suitable analytical methods. Thus, in this paper, different phosphopeptide enrichment strategies were pursued, based either on metal oxide affinity chromatography (MOAC, in the form of commercial TiO
2
spin columns or magnetic graphitized carbon black-TiO
2
composite), or on immobilized metal ion affinity chromatography (IMAC, in the form of Ti
4+
-IMAC magnetic material or commercial Fe
3+
-IMAC spin columns). While MOAC strategies proved completely unsuccessful, probably due to interfering phospholipids displacing phosphopeptides, the IMAC materials performed very well. Different sample preparation strategies were tested, comprising direct dilution with the loading buffer, organic solvent precipitation, and lipid removal from the matrix, as well as the addition of phosphatase inhibitors during sample handling for maximized endogenous phosphopeptide enrichment. All data were acquired by a shotgun peptidomics approach, in which peptide samples were separated by reversed-phase nanoHPLC hyphenated with high-resolution tandem mass spectrometry. The devised method allowed the identification of 176 endogenous phosphopeptides in fresh serum added with inhibitors by the direct dilution protocol and the Ti
4+
-IMAC magnetic material enrichment, but good results could also be obtained from the commercial Fe
3+
-IMAC spin column adapted to the batch enrichment protocol. |
| doi_str_mv | 10.1007/s00216-017-0822-8 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_1989556602</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A523919757</galeid><sourcerecordid>A523919757</sourcerecordid><originalsourceid>FETCH-LOGICAL-c504t-2f8150a508593b127922bab43227517566e5d616a46667b1fe4751a6d0a969663</originalsourceid><addsrcrecordid>eNp9Uctu1TAUjBAVLYUPYIMisWGT4nMSv5ZVeUqV2LRry0lOblwldrATpPL1-HLb8hAgy7I1nhmPPUXxAtgZMCbfJMYQRMVAVkwhVupRcQICVIWCs8cP-waPi6cp3TAGXIF4UhyjrkHVAk4K-5a-0hSWmfxahqG0viQfXTf-AGZax9CXQ4gZ7cOOfNhSuYwh5bnQsrqeym600XYrRffNri740vly3ObslChu87PiaLBToud362lx_f7d1cXH6vLzh08X55dVx1mzVjgo4MxypriuW0CpEVvbNjWi5CC5EMR7AcI2QgjZwkBNxq3omdVCC1GfFq8PvksMXzZKq5ld6miarKec2oBWmmcbhpn66g_qTdiiz-kMcgDJUCH_Hwu0Rqn2SX6ydnYi4_wQ1vwb-6vNOcdag5ZcZtbZX1h59DS7LngaXMZ_E8BB0MWQUqTBLNHNNt4aYGZfvjmUb3L5Zl--UVnz8i7w1s7UPyju284EPBBSPvI7ir-86J-u3wE-W7ZX</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1992784666</pqid></control><display><type>article</type><title>Development of an enrichment method for endogenous phosphopeptide characterization in human serum</title><source>SpringerNature Journals</source><creator>La Barbera, Giorgia ; Capriotti, Anna Laura ; Cavaliere, Chiara ; Ferraris, Francesca ; Laus, Michele ; Piovesana, Susy ; Sparnacci, Katia ; Laganà, Aldo</creator><creatorcontrib>La Barbera, Giorgia ; Capriotti, Anna Laura ; Cavaliere, Chiara ; Ferraris, Francesca ; Laus, Michele ; Piovesana, Susy ; Sparnacci, Katia ; Laganà, Aldo</creatorcontrib><description>The work describes the development of an enrichment method for the analysis of endogenous phosphopeptides in serum. Endogenous peptides can play significant biological roles, and some of them could be exploited as future biomarkers. In this context, blood is one of the most useful biofluids for screening, but a systematic investigation of the endogenous peptides, especially phosphorylated ones, is still lacking, mainly due to the lack of suitable analytical methods. Thus, in this paper, different phosphopeptide enrichment strategies were pursued, based either on metal oxide affinity chromatography (MOAC, in the form of commercial TiO
2
spin columns or magnetic graphitized carbon black-TiO
2
composite), or on immobilized metal ion affinity chromatography (IMAC, in the form of Ti
4+
-IMAC magnetic material or commercial Fe
3+
-IMAC spin columns). While MOAC strategies proved completely unsuccessful, probably due to interfering phospholipids displacing phosphopeptides, the IMAC materials performed very well. Different sample preparation strategies were tested, comprising direct dilution with the loading buffer, organic solvent precipitation, and lipid removal from the matrix, as well as the addition of phosphatase inhibitors during sample handling for maximized endogenous phosphopeptide enrichment. All data were acquired by a shotgun peptidomics approach, in which peptide samples were separated by reversed-phase nanoHPLC hyphenated with high-resolution tandem mass spectrometry. The devised method allowed the identification of 176 endogenous phosphopeptides in fresh serum added with inhibitors by the direct dilution protocol and the Ti
4+
-IMAC magnetic material enrichment, but good results could also be obtained from the commercial Fe
3+
-IMAC spin column adapted to the batch enrichment protocol.</description><identifier>ISSN: 1618-2642</identifier><identifier>EISSN: 1618-2650</identifier><identifier>DOI: 10.1007/s00216-017-0822-8</identifier><identifier>PMID: 29318361</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>ABCs 16th Anniversary ; Affinity ; Affinity chromatography ; Analytical Chemistry ; Biochemistry ; Biomarkers ; Black carbon ; Blood serum ; Carbon black ; Characterization and Evaluation of Materials ; Chemical properties ; Chemistry ; Chemistry and Materials Science ; Chromatography ; Composite materials ; Composition ; Data acquisition ; Dilution ; Enrichment ; Ferric ions ; Food Science ; Graphitization ; Identification and classification ; Inhibitors ; Iron ; Laboratory Medicine ; Lipids ; Liquid chromatography ; Magnetic materials ; Mass spectrometry ; Mass spectroscopy ; Matrix algebra ; Metal ions ; Metal oxides ; Methods ; Monitoring/Environmental Analysis ; Peptides ; Phospholipids ; Research Paper ; Sample preparation ; Shotguns ; Titanium dioxide</subject><ispartof>Analytical and bioanalytical chemistry, 2018-01, Vol.410 (3), p.1177-1185</ispartof><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2018</rights><rights>COPYRIGHT 2018 Springer</rights><rights>Analytical and Bioanalytical Chemistry is a copyright of Springer, (2018). All Rights Reserved.</rights><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2018.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c504t-2f8150a508593b127922bab43227517566e5d616a46667b1fe4751a6d0a969663</citedby><cites>FETCH-LOGICAL-c504t-2f8150a508593b127922bab43227517566e5d616a46667b1fe4751a6d0a969663</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00216-017-0822-8$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00216-017-0822-8$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29318361$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>La Barbera, Giorgia</creatorcontrib><creatorcontrib>Capriotti, Anna Laura</creatorcontrib><creatorcontrib>Cavaliere, Chiara</creatorcontrib><creatorcontrib>Ferraris, Francesca</creatorcontrib><creatorcontrib>Laus, Michele</creatorcontrib><creatorcontrib>Piovesana, Susy</creatorcontrib><creatorcontrib>Sparnacci, Katia</creatorcontrib><creatorcontrib>Laganà, Aldo</creatorcontrib><title>Development of an enrichment method for endogenous phosphopeptide characterization in human serum</title><title>Analytical and bioanalytical chemistry</title><addtitle>Anal Bioanal Chem</addtitle><addtitle>Anal Bioanal Chem</addtitle><description>The work describes the development of an enrichment method for the analysis of endogenous phosphopeptides in serum. Endogenous peptides can play significant biological roles, and some of them could be exploited as future biomarkers. In this context, blood is one of the most useful biofluids for screening, but a systematic investigation of the endogenous peptides, especially phosphorylated ones, is still lacking, mainly due to the lack of suitable analytical methods. Thus, in this paper, different phosphopeptide enrichment strategies were pursued, based either on metal oxide affinity chromatography (MOAC, in the form of commercial TiO
2
spin columns or magnetic graphitized carbon black-TiO
2
composite), or on immobilized metal ion affinity chromatography (IMAC, in the form of Ti
4+
-IMAC magnetic material or commercial Fe
3+
-IMAC spin columns). While MOAC strategies proved completely unsuccessful, probably due to interfering phospholipids displacing phosphopeptides, the IMAC materials performed very well. Different sample preparation strategies were tested, comprising direct dilution with the loading buffer, organic solvent precipitation, and lipid removal from the matrix, as well as the addition of phosphatase inhibitors during sample handling for maximized endogenous phosphopeptide enrichment. All data were acquired by a shotgun peptidomics approach, in which peptide samples were separated by reversed-phase nanoHPLC hyphenated with high-resolution tandem mass spectrometry. The devised method allowed the identification of 176 endogenous phosphopeptides in fresh serum added with inhibitors by the direct dilution protocol and the Ti
4+
-IMAC magnetic material enrichment, but good results could also be obtained from the commercial Fe
3+
-IMAC spin column adapted to the batch enrichment protocol.</description><subject>ABCs 16th Anniversary</subject><subject>Affinity</subject><subject>Affinity chromatography</subject><subject>Analytical Chemistry</subject><subject>Biochemistry</subject><subject>Biomarkers</subject><subject>Black carbon</subject><subject>Blood serum</subject><subject>Carbon black</subject><subject>Characterization and Evaluation of Materials</subject><subject>Chemical properties</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chromatography</subject><subject>Composite materials</subject><subject>Composition</subject><subject>Data acquisition</subject><subject>Dilution</subject><subject>Enrichment</subject><subject>Ferric ions</subject><subject>Food Science</subject><subject>Graphitization</subject><subject>Identification and classification</subject><subject>Inhibitors</subject><subject>Iron</subject><subject>Laboratory Medicine</subject><subject>Lipids</subject><subject>Liquid chromatography</subject><subject>Magnetic materials</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Matrix algebra</subject><subject>Metal ions</subject><subject>Metal oxides</subject><subject>Methods</subject><subject>Monitoring/Environmental Analysis</subject><subject>Peptides</subject><subject>Phospholipids</subject><subject>Research Paper</subject><subject>Sample preparation</subject><subject>Shotguns</subject><subject>Titanium dioxide</subject><issn>1618-2642</issn><issn>1618-2650</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9Uctu1TAUjBAVLYUPYIMisWGT4nMSv5ZVeUqV2LRry0lOblwldrATpPL1-HLb8hAgy7I1nhmPPUXxAtgZMCbfJMYQRMVAVkwhVupRcQICVIWCs8cP-waPi6cp3TAGXIF4UhyjrkHVAk4K-5a-0hSWmfxahqG0viQfXTf-AGZax9CXQ4gZ7cOOfNhSuYwh5bnQsrqeym600XYrRffNri740vly3ObslChu87PiaLBToud362lx_f7d1cXH6vLzh08X55dVx1mzVjgo4MxypriuW0CpEVvbNjWi5CC5EMR7AcI2QgjZwkBNxq3omdVCC1GfFq8PvksMXzZKq5ld6miarKec2oBWmmcbhpn66g_qTdiiz-kMcgDJUCH_Hwu0Rqn2SX6ydnYi4_wQ1vwb-6vNOcdag5ZcZtbZX1h59DS7LngaXMZ_E8BB0MWQUqTBLNHNNt4aYGZfvjmUb3L5Zl--UVnz8i7w1s7UPyju284EPBBSPvI7ir-86J-u3wE-W7ZX</recordid><startdate>20180101</startdate><enddate>20180101</enddate><creator>La Barbera, Giorgia</creator><creator>Capriotti, Anna Laura</creator><creator>Cavaliere, Chiara</creator><creator>Ferraris, Francesca</creator><creator>Laus, Michele</creator><creator>Piovesana, Susy</creator><creator>Sparnacci, Katia</creator><creator>Laganà, Aldo</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7TA</scope><scope>7TB</scope><scope>7U5</scope><scope>7U7</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>F28</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H8D</scope><scope>H8G</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KB.</scope><scope>KR7</scope><scope>L7M</scope><scope>LK8</scope><scope>L~C</scope><scope>L~D</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope></search><sort><creationdate>20180101</creationdate><title>Development of an enrichment method for endogenous phosphopeptide characterization in human serum</title><author>La Barbera, Giorgia ; Capriotti, Anna Laura ; Cavaliere, Chiara ; Ferraris, Francesca ; Laus, Michele ; Piovesana, Susy ; Sparnacci, Katia ; Laganà, Aldo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c504t-2f8150a508593b127922bab43227517566e5d616a46667b1fe4751a6d0a969663</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>ABCs 16th Anniversary</topic><topic>Affinity</topic><topic>Affinity chromatography</topic><topic>Analytical Chemistry</topic><topic>Biochemistry</topic><topic>Biomarkers</topic><topic>Black carbon</topic><topic>Blood serum</topic><topic>Carbon black</topic><topic>Characterization and Evaluation of Materials</topic><topic>Chemical properties</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chromatography</topic><topic>Composite materials</topic><topic>Composition</topic><topic>Data acquisition</topic><topic>Dilution</topic><topic>Enrichment</topic><topic>Ferric ions</topic><topic>Food Science</topic><topic>Graphitization</topic><topic>Identification and classification</topic><topic>Inhibitors</topic><topic>Iron</topic><topic>Laboratory Medicine</topic><topic>Lipids</topic><topic>Liquid chromatography</topic><topic>Magnetic materials</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Matrix algebra</topic><topic>Metal ions</topic><topic>Metal oxides</topic><topic>Methods</topic><topic>Monitoring/Environmental Analysis</topic><topic>Peptides</topic><topic>Phospholipids</topic><topic>Research Paper</topic><topic>Sample preparation</topic><topic>Shotguns</topic><topic>Titanium dioxide</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>La Barbera, Giorgia</creatorcontrib><creatorcontrib>Capriotti, Anna Laura</creatorcontrib><creatorcontrib>Cavaliere, Chiara</creatorcontrib><creatorcontrib>Ferraris, Francesca</creatorcontrib><creatorcontrib>Laus, Michele</creatorcontrib><creatorcontrib>Piovesana, Susy</creatorcontrib><creatorcontrib>Sparnacci, Katia</creatorcontrib><creatorcontrib>Laganà, Aldo</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>SciTech Premium Collection</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>ProQuest Biological Science Collection</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>MEDLINE - Academic</collection><jtitle>Analytical and bioanalytical chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>La Barbera, Giorgia</au><au>Capriotti, Anna Laura</au><au>Cavaliere, Chiara</au><au>Ferraris, Francesca</au><au>Laus, Michele</au><au>Piovesana, Susy</au><au>Sparnacci, Katia</au><au>Laganà, Aldo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Development of an enrichment method for endogenous phosphopeptide characterization in human serum</atitle><jtitle>Analytical and bioanalytical chemistry</jtitle><stitle>Anal Bioanal Chem</stitle><addtitle>Anal Bioanal Chem</addtitle><date>2018-01-01</date><risdate>2018</risdate><volume>410</volume><issue>3</issue><spage>1177</spage><epage>1185</epage><pages>1177-1185</pages><issn>1618-2642</issn><eissn>1618-2650</eissn><abstract>The work describes the development of an enrichment method for the analysis of endogenous phosphopeptides in serum. Endogenous peptides can play significant biological roles, and some of them could be exploited as future biomarkers. In this context, blood is one of the most useful biofluids for screening, but a systematic investigation of the endogenous peptides, especially phosphorylated ones, is still lacking, mainly due to the lack of suitable analytical methods. Thus, in this paper, different phosphopeptide enrichment strategies were pursued, based either on metal oxide affinity chromatography (MOAC, in the form of commercial TiO
2
spin columns or magnetic graphitized carbon black-TiO
2
composite), or on immobilized metal ion affinity chromatography (IMAC, in the form of Ti
4+
-IMAC magnetic material or commercial Fe
3+
-IMAC spin columns). While MOAC strategies proved completely unsuccessful, probably due to interfering phospholipids displacing phosphopeptides, the IMAC materials performed very well. Different sample preparation strategies were tested, comprising direct dilution with the loading buffer, organic solvent precipitation, and lipid removal from the matrix, as well as the addition of phosphatase inhibitors during sample handling for maximized endogenous phosphopeptide enrichment. All data were acquired by a shotgun peptidomics approach, in which peptide samples were separated by reversed-phase nanoHPLC hyphenated with high-resolution tandem mass spectrometry. The devised method allowed the identification of 176 endogenous phosphopeptides in fresh serum added with inhibitors by the direct dilution protocol and the Ti
4+
-IMAC magnetic material enrichment, but good results could also be obtained from the commercial Fe
3+
-IMAC spin column adapted to the batch enrichment protocol.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>29318361</pmid><doi>10.1007/s00216-017-0822-8</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1618-2642 |
| ispartof | Analytical and bioanalytical chemistry, 2018-01, Vol.410 (3), p.1177-1185 |
| issn | 1618-2642 1618-2650 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1989556602 |
| source | SpringerNature Journals |
| subjects | ABCs 16th Anniversary Affinity Affinity chromatography Analytical Chemistry Biochemistry Biomarkers Black carbon Blood serum Carbon black Characterization and Evaluation of Materials Chemical properties Chemistry Chemistry and Materials Science Chromatography Composite materials Composition Data acquisition Dilution Enrichment Ferric ions Food Science Graphitization Identification and classification Inhibitors Iron Laboratory Medicine Lipids Liquid chromatography Magnetic materials Mass spectrometry Mass spectroscopy Matrix algebra Metal ions Metal oxides Methods Monitoring/Environmental Analysis Peptides Phospholipids Research Paper Sample preparation Shotguns Titanium dioxide |
| title | Development of an enrichment method for endogenous phosphopeptide characterization in human serum |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-29T11%3A19%3A24IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Development%20of%20an%20enrichment%20method%20for%20endogenous%20phosphopeptide%20characterization%20in%20human%20serum&rft.jtitle=Analytical%20and%20bioanalytical%20chemistry&rft.au=La%20Barbera,%20Giorgia&rft.date=2018-01-01&rft.volume=410&rft.issue=3&rft.spage=1177&rft.epage=1185&rft.pages=1177-1185&rft.issn=1618-2642&rft.eissn=1618-2650&rft_id=info:doi/10.1007/s00216-017-0822-8&rft_dat=%3Cgale_proqu%3EA523919757%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1992784666&rft_id=info:pmid/29318361&rft_galeid=A523919757&rfr_iscdi=true |