Comparative Quantitation of Aberrant Glycoforms by Lectin-Based Glycoprotein Enrichment Coupled with Multiple-Reaction Monitoring Mass Spectrometry
Lectin enrichment-coupled multiple-reaction monitoring (MRM) mass spectrometry was employed to quantitatively monitor the variation of aberrant glycoforms produced under pathological states. For this, aberrant glycoforms of the tissue inhibitor of metalloproteinase 1 (TIMP1) and protein tyrosine pho...
Gespeichert in:
| Veröffentlicht in: | Analytical chemistry (Washington) 2010-06, Vol.82 (11), p.4441-4447 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 4447 |
|---|---|
| container_issue | 11 |
| container_start_page | 4441 |
| container_title | Analytical chemistry (Washington) |
| container_volume | 82 |
| creator | Ahn, Yeong Hee Kim, Yong-Sam Ji, Eun Sun Lee, Ji Yeon Jung, Ji-Ae Ko, Jeong Heon Yoo, Jong Shin |
| description | Lectin enrichment-coupled multiple-reaction monitoring (MRM) mass spectrometry was employed to quantitatively monitor the variation of aberrant glycoforms produced under pathological states. For this, aberrant glycoforms of the tissue inhibitor of metalloproteinase 1 (TIMP1) and protein tyrosine phosphatase κ (PTPκ), previously known target proteins for N-acetylglucosaminyltransferase-V (GnT-V), were enriched by phytohemagglutinin-L4 (L-PHA) lectin and comparatively analyzed in the conditioned medium of the WiDr colon cancer cell line and its GnT-V-overexpressing transfectant cells. Enriched glycoforms were digested, and the resultant peptides were comparatively quantified by MRM analysis. MRM quantitation data for the L-PHA-enriched samples revealed that the abundance of aberrant glycoforms of TIMP1 and PTPκ was greatly increased (11.7- and 16.5-fold, respectively) in GnT-V-treated cells compared to the control cells, although the abundance of total TIMP1 and PTPκ in GnT-V-treated cells was slightly different (1.1- and 0.5-fold, respectively) for unenriched samples compared to that in control cells. The dramatic variation in abundance of the aberrant glycoforms due to overexpressed GnT-V was confirmed quantitatively by comparative MRM analysis of lectin-enriched samples. This method is capable of comparatively quantitating the abundance of a protein of interest and its aberrant glycoform and will be useful for studying pathological mechanisms of cancer or verifying biomarker candidates. |
| doi_str_mv | 10.1021/ac1001965 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_733108180</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2066506101</sourcerecordid><originalsourceid>FETCH-LOGICAL-a371t-a8f6f38522e403358d40b9c4aa5bd61a20203291caedd988212d2db0f7ee9bc3</originalsourceid><addsrcrecordid>eNplkd2KFDEQhYMo7rh64QtIEES8aK0k_Xu5O6yrMIOoe99Up6vdLN1Jm6SVeQ5f2Iwz7oBehUp9depQh7HnAt4KkOIdagEgmrJ4wFaikJCVdS0fshUAqExWAGfsSQh3iREgysfsTEJeSlEVK_Zr7aYZPUbzg_jnBW00MRXOcjfwi468T1_8etxpNzg_Bd7t-IZ0NDa7xED9oTV7F8lYfmW90bcTpZG1W-Yx9X-aeMu3yxhNKrMvhPqP-tZZE5039hvfYgj865xEvZso-t1T9mjAMdCz43vObt5f3aw_ZJtP1x_XF5sMVSVihvVQDqoupKQclCrqPoeu0Tli0fWlQAkSlGyERur7Jl1EyF72HQwVUdNpdc5eH2ST--8LhdhOJmgaR7TkltBWSgmoRQ2JfPkPeecWb5O3tthvEbLZQ28OkPYuBE9DO3szod-1Atp9TO19TIl9cRRcuon6e_JvLgl4dQQwaByHlII24cTJOi-LpjpxqMPJ1P8LfwO7KafA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>520201290</pqid></control><display><type>article</type><title>Comparative Quantitation of Aberrant Glycoforms by Lectin-Based Glycoprotein Enrichment Coupled with Multiple-Reaction Monitoring Mass Spectrometry</title><source>ACS Publications</source><source>MEDLINE</source><creator>Ahn, Yeong Hee ; Kim, Yong-Sam ; Ji, Eun Sun ; Lee, Ji Yeon ; Jung, Ji-Ae ; Ko, Jeong Heon ; Yoo, Jong Shin</creator><creatorcontrib>Ahn, Yeong Hee ; Kim, Yong-Sam ; Ji, Eun Sun ; Lee, Ji Yeon ; Jung, Ji-Ae ; Ko, Jeong Heon ; Yoo, Jong Shin</creatorcontrib><description>Lectin enrichment-coupled multiple-reaction monitoring (MRM) mass spectrometry was employed to quantitatively monitor the variation of aberrant glycoforms produced under pathological states. For this, aberrant glycoforms of the tissue inhibitor of metalloproteinase 1 (TIMP1) and protein tyrosine phosphatase κ (PTPκ), previously known target proteins for N-acetylglucosaminyltransferase-V (GnT-V), were enriched by phytohemagglutinin-L4 (L-PHA) lectin and comparatively analyzed in the conditioned medium of the WiDr colon cancer cell line and its GnT-V-overexpressing transfectant cells. Enriched glycoforms were digested, and the resultant peptides were comparatively quantified by MRM analysis. MRM quantitation data for the L-PHA-enriched samples revealed that the abundance of aberrant glycoforms of TIMP1 and PTPκ was greatly increased (11.7- and 16.5-fold, respectively) in GnT-V-treated cells compared to the control cells, although the abundance of total TIMP1 and PTPκ in GnT-V-treated cells was slightly different (1.1- and 0.5-fold, respectively) for unenriched samples compared to that in control cells. The dramatic variation in abundance of the aberrant glycoforms due to overexpressed GnT-V was confirmed quantitatively by comparative MRM analysis of lectin-enriched samples. This method is capable of comparatively quantitating the abundance of a protein of interest and its aberrant glycoform and will be useful for studying pathological mechanisms of cancer or verifying biomarker candidates.</description><identifier>ISSN: 0003-2700</identifier><identifier>EISSN: 1520-6882</identifier><identifier>DOI: 10.1021/ac1001965</identifier><identifier>PMID: 20462175</identifier><identifier>CODEN: ANCHAM</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Amino Acid Sequence ; Analytical chemistry ; Biochemistry ; Biomarkers ; Calibration ; Cell Line, Tumor ; Chemistry ; Colorectal cancer ; Desmoglein 2 - metabolism ; Exact sciences and technology ; Gene expression ; Glycoproteins ; Glycoproteins - chemistry ; Glycoproteins - metabolism ; Glycosylation ; Humans ; Lectins - metabolism ; Mass spectrometry ; Mass Spectrometry - methods ; Molecular Sequence Data ; N-Acetylglucosaminyltransferases - metabolism ; Peptides ; Peptides - chemistry ; Peptides - metabolism ; Phytohemagglutinins - metabolism ; Protein Tyrosine Phosphatases - metabolism ; Proteins ; Spectrometric and optical methods ; Tissue Inhibitor of Metalloproteinase-1 - metabolism ; Trypsin - metabolism</subject><ispartof>Analytical chemistry (Washington), 2010-06, Vol.82 (11), p.4441-4447</ispartof><rights>Copyright © 2010 American Chemical Society</rights><rights>2015 INIST-CNRS</rights><rights>Copyright American Chemical Society Jun 1, 2010</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a371t-a8f6f38522e403358d40b9c4aa5bd61a20203291caedd988212d2db0f7ee9bc3</citedby><cites>FETCH-LOGICAL-a371t-a8f6f38522e403358d40b9c4aa5bd61a20203291caedd988212d2db0f7ee9bc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/ac1001965$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/ac1001965$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22846597$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20462175$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ahn, Yeong Hee</creatorcontrib><creatorcontrib>Kim, Yong-Sam</creatorcontrib><creatorcontrib>Ji, Eun Sun</creatorcontrib><creatorcontrib>Lee, Ji Yeon</creatorcontrib><creatorcontrib>Jung, Ji-Ae</creatorcontrib><creatorcontrib>Ko, Jeong Heon</creatorcontrib><creatorcontrib>Yoo, Jong Shin</creatorcontrib><title>Comparative Quantitation of Aberrant Glycoforms by Lectin-Based Glycoprotein Enrichment Coupled with Multiple-Reaction Monitoring Mass Spectrometry</title><title>Analytical chemistry (Washington)</title><addtitle>Anal. Chem</addtitle><description>Lectin enrichment-coupled multiple-reaction monitoring (MRM) mass spectrometry was employed to quantitatively monitor the variation of aberrant glycoforms produced under pathological states. For this, aberrant glycoforms of the tissue inhibitor of metalloproteinase 1 (TIMP1) and protein tyrosine phosphatase κ (PTPκ), previously known target proteins for N-acetylglucosaminyltransferase-V (GnT-V), were enriched by phytohemagglutinin-L4 (L-PHA) lectin and comparatively analyzed in the conditioned medium of the WiDr colon cancer cell line and its GnT-V-overexpressing transfectant cells. Enriched glycoforms were digested, and the resultant peptides were comparatively quantified by MRM analysis. MRM quantitation data for the L-PHA-enriched samples revealed that the abundance of aberrant glycoforms of TIMP1 and PTPκ was greatly increased (11.7- and 16.5-fold, respectively) in GnT-V-treated cells compared to the control cells, although the abundance of total TIMP1 and PTPκ in GnT-V-treated cells was slightly different (1.1- and 0.5-fold, respectively) for unenriched samples compared to that in control cells. The dramatic variation in abundance of the aberrant glycoforms due to overexpressed GnT-V was confirmed quantitatively by comparative MRM analysis of lectin-enriched samples. This method is capable of comparatively quantitating the abundance of a protein of interest and its aberrant glycoform and will be useful for studying pathological mechanisms of cancer or verifying biomarker candidates.</description><subject>Amino Acid Sequence</subject><subject>Analytical chemistry</subject><subject>Biochemistry</subject><subject>Biomarkers</subject><subject>Calibration</subject><subject>Cell Line, Tumor</subject><subject>Chemistry</subject><subject>Colorectal cancer</subject><subject>Desmoglein 2 - metabolism</subject><subject>Exact sciences and technology</subject><subject>Gene expression</subject><subject>Glycoproteins</subject><subject>Glycoproteins - chemistry</subject><subject>Glycoproteins - metabolism</subject><subject>Glycosylation</subject><subject>Humans</subject><subject>Lectins - metabolism</subject><subject>Mass spectrometry</subject><subject>Mass Spectrometry - methods</subject><subject>Molecular Sequence Data</subject><subject>N-Acetylglucosaminyltransferases - metabolism</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Peptides - metabolism</subject><subject>Phytohemagglutinins - metabolism</subject><subject>Protein Tyrosine Phosphatases - metabolism</subject><subject>Proteins</subject><subject>Spectrometric and optical methods</subject><subject>Tissue Inhibitor of Metalloproteinase-1 - metabolism</subject><subject>Trypsin - metabolism</subject><issn>0003-2700</issn><issn>1520-6882</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNplkd2KFDEQhYMo7rh64QtIEES8aK0k_Xu5O6yrMIOoe99Up6vdLN1Jm6SVeQ5f2Iwz7oBehUp9depQh7HnAt4KkOIdagEgmrJ4wFaikJCVdS0fshUAqExWAGfsSQh3iREgysfsTEJeSlEVK_Zr7aYZPUbzg_jnBW00MRXOcjfwi468T1_8etxpNzg_Bd7t-IZ0NDa7xED9oTV7F8lYfmW90bcTpZG1W-Yx9X-aeMu3yxhNKrMvhPqP-tZZE5039hvfYgj865xEvZso-t1T9mjAMdCz43vObt5f3aw_ZJtP1x_XF5sMVSVihvVQDqoupKQclCrqPoeu0Tli0fWlQAkSlGyERur7Jl1EyF72HQwVUdNpdc5eH2ST--8LhdhOJmgaR7TkltBWSgmoRQ2JfPkPeecWb5O3tthvEbLZQ28OkPYuBE9DO3szod-1Atp9TO19TIl9cRRcuon6e_JvLgl4dQQwaByHlII24cTJOi-LpjpxqMPJ1P8LfwO7KafA</recordid><startdate>20100601</startdate><enddate>20100601</enddate><creator>Ahn, Yeong Hee</creator><creator>Kim, Yong-Sam</creator><creator>Ji, Eun Sun</creator><creator>Lee, Ji Yeon</creator><creator>Jung, Ji-Ae</creator><creator>Ko, Jeong Heon</creator><creator>Yoo, Jong Shin</creator><general>American Chemical Society</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</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>7TM</scope><scope>7U5</scope><scope>7U7</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20100601</creationdate><title>Comparative Quantitation of Aberrant Glycoforms by Lectin-Based Glycoprotein Enrichment Coupled with Multiple-Reaction Monitoring Mass Spectrometry</title><author>Ahn, Yeong Hee ; Kim, Yong-Sam ; Ji, Eun Sun ; Lee, Ji Yeon ; Jung, Ji-Ae ; Ko, Jeong Heon ; Yoo, Jong Shin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a371t-a8f6f38522e403358d40b9c4aa5bd61a20203291caedd988212d2db0f7ee9bc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical chemistry</topic><topic>Biochemistry</topic><topic>Biomarkers</topic><topic>Calibration</topic><topic>Cell Line, Tumor</topic><topic>Chemistry</topic><topic>Colorectal cancer</topic><topic>Desmoglein 2 - metabolism</topic><topic>Exact sciences and technology</topic><topic>Gene expression</topic><topic>Glycoproteins</topic><topic>Glycoproteins - chemistry</topic><topic>Glycoproteins - metabolism</topic><topic>Glycosylation</topic><topic>Humans</topic><topic>Lectins - metabolism</topic><topic>Mass spectrometry</topic><topic>Mass Spectrometry - methods</topic><topic>Molecular Sequence Data</topic><topic>N-Acetylglucosaminyltransferases - metabolism</topic><topic>Peptides</topic><topic>Peptides - chemistry</topic><topic>Peptides - metabolism</topic><topic>Phytohemagglutinins - metabolism</topic><topic>Protein Tyrosine Phosphatases - metabolism</topic><topic>Proteins</topic><topic>Spectrometric and optical methods</topic><topic>Tissue Inhibitor of Metalloproteinase-1 - metabolism</topic><topic>Trypsin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ahn, Yeong Hee</creatorcontrib><creatorcontrib>Kim, Yong-Sam</creatorcontrib><creatorcontrib>Ji, Eun Sun</creatorcontrib><creatorcontrib>Lee, Ji Yeon</creatorcontrib><creatorcontrib>Jung, Ji-Ae</creatorcontrib><creatorcontrib>Ko, Jeong Heon</creatorcontrib><creatorcontrib>Yoo, Jong Shin</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</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>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Analytical chemistry (Washington)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ahn, Yeong Hee</au><au>Kim, Yong-Sam</au><au>Ji, Eun Sun</au><au>Lee, Ji Yeon</au><au>Jung, Ji-Ae</au><au>Ko, Jeong Heon</au><au>Yoo, Jong Shin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparative Quantitation of Aberrant Glycoforms by Lectin-Based Glycoprotein Enrichment Coupled with Multiple-Reaction Monitoring Mass Spectrometry</atitle><jtitle>Analytical chemistry (Washington)</jtitle><addtitle>Anal. Chem</addtitle><date>2010-06-01</date><risdate>2010</risdate><volume>82</volume><issue>11</issue><spage>4441</spage><epage>4447</epage><pages>4441-4447</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><coden>ANCHAM</coden><abstract>Lectin enrichment-coupled multiple-reaction monitoring (MRM) mass spectrometry was employed to quantitatively monitor the variation of aberrant glycoforms produced under pathological states. For this, aberrant glycoforms of the tissue inhibitor of metalloproteinase 1 (TIMP1) and protein tyrosine phosphatase κ (PTPκ), previously known target proteins for N-acetylglucosaminyltransferase-V (GnT-V), were enriched by phytohemagglutinin-L4 (L-PHA) lectin and comparatively analyzed in the conditioned medium of the WiDr colon cancer cell line and its GnT-V-overexpressing transfectant cells. Enriched glycoforms were digested, and the resultant peptides were comparatively quantified by MRM analysis. MRM quantitation data for the L-PHA-enriched samples revealed that the abundance of aberrant glycoforms of TIMP1 and PTPκ was greatly increased (11.7- and 16.5-fold, respectively) in GnT-V-treated cells compared to the control cells, although the abundance of total TIMP1 and PTPκ in GnT-V-treated cells was slightly different (1.1- and 0.5-fold, respectively) for unenriched samples compared to that in control cells. The dramatic variation in abundance of the aberrant glycoforms due to overexpressed GnT-V was confirmed quantitatively by comparative MRM analysis of lectin-enriched samples. This method is capable of comparatively quantitating the abundance of a protein of interest and its aberrant glycoform and will be useful for studying pathological mechanisms of cancer or verifying biomarker candidates.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>20462175</pmid><doi>10.1021/ac1001965</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-2700 |
| ispartof | Analytical chemistry (Washington), 2010-06, Vol.82 (11), p.4441-4447 |
| issn | 0003-2700 1520-6882 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_733108180 |
| source | ACS Publications; MEDLINE |
| subjects | Amino Acid Sequence Analytical chemistry Biochemistry Biomarkers Calibration Cell Line, Tumor Chemistry Colorectal cancer Desmoglein 2 - metabolism Exact sciences and technology Gene expression Glycoproteins Glycoproteins - chemistry Glycoproteins - metabolism Glycosylation Humans Lectins - metabolism Mass spectrometry Mass Spectrometry - methods Molecular Sequence Data N-Acetylglucosaminyltransferases - metabolism Peptides Peptides - chemistry Peptides - metabolism Phytohemagglutinins - metabolism Protein Tyrosine Phosphatases - metabolism Proteins Spectrometric and optical methods Tissue Inhibitor of Metalloproteinase-1 - metabolism Trypsin - metabolism |
| title | Comparative Quantitation of Aberrant Glycoforms by Lectin-Based Glycoprotein Enrichment Coupled with Multiple-Reaction Monitoring Mass Spectrometry |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-10T20%3A32%3A57IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Comparative%20Quantitation%20of%20Aberrant%20Glycoforms%20by%20Lectin-Based%20Glycoprotein%20Enrichment%20Coupled%20with%20Multiple-Reaction%20Monitoring%20Mass%20Spectrometry&rft.jtitle=Analytical%20chemistry%20(Washington)&rft.au=Ahn,%20Yeong%20Hee&rft.date=2010-06-01&rft.volume=82&rft.issue=11&rft.spage=4441&rft.epage=4447&rft.pages=4441-4447&rft.issn=0003-2700&rft.eissn=1520-6882&rft.coden=ANCHAM&rft_id=info:doi/10.1021/ac1001965&rft_dat=%3Cproquest_cross%3E2066506101%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=520201290&rft_id=info:pmid/20462175&rfr_iscdi=true |