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Profile of native N-linked glycan structures from human serum using high performance liquid chromatography on a microfluidic chip and time-of-flight mass spectrometry
Protein glycosylation involves the addition of monosaccharides in a stepwise process requiring no glycan template. Therefore, identifying the numerous glycoforms, including isomers, can help elucidate the biological function(s) of particular glycans. A method to assess the diversity of the N-linked...
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Published in: | Proteomics (Weinheim) 2009-04, Vol.9 (7), p.1939-1951 |
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container_end_page | 1951 |
container_issue | 7 |
container_start_page | 1939 |
container_title | Proteomics (Weinheim) |
container_volume | 9 |
creator | Chu, Caroline S Niñonuevo, Milady R Clowers, Brian H Perkins, Patrick D An, Hyun Joo Yin, Hongfeng Killeen, Kevin Miyamoto, Suzanne Grimm, Rudolf Lebrilla, Carlito B |
description | Protein glycosylation involves the addition of monosaccharides in a stepwise process requiring no glycan template. Therefore, identifying the numerous glycoforms, including isomers, can help elucidate the biological function(s) of particular glycans. A method to assess the diversity of the N-linked oligosaccharides released from human serum without derivatization has been developed using on-line nanoLC and high resolution TOF MS. The N-linked oligosaccharides were analyzed with MALDI FT-ICR MS and microchip LC MS (HPLC-Chip/TOF MS). Two microfluidic chips were employed, the glycan chip (40 nL enrichment column, 43x0.075 mm² i.d. analytical column) and the high capacity chip (160 nL enrichment column, 140x0.075 mm² i.d. analytical column), both with graphitized carbon as the stationary phase. Both chips offered good sensitivity and reproducibility in separating a heterogeneous mixture of neutral and anionic oligosaccharides between injections. Increasing the length and volume of the enrichment and the analytical columns improved resolution of the peaks. Complex type N-linked oligosaccharides were the most abundant oligosaccharides in human serum accounting for ~96% of the total glycans identified, while hybrid and high mannose type oligosaccharides comprise the remaining ~4%. |
doi_str_mv | 10.1002/pmic.200800249 |
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Therefore, identifying the numerous glycoforms, including isomers, can help elucidate the biological function(s) of particular glycans. A method to assess the diversity of the N-linked oligosaccharides released from human serum without derivatization has been developed using on-line nanoLC and high resolution TOF MS. The N-linked oligosaccharides were analyzed with MALDI FT-ICR MS and microchip LC MS (HPLC-Chip/TOF MS). Two microfluidic chips were employed, the glycan chip (40 nL enrichment column, 43x0.075 mm² i.d. analytical column) and the high capacity chip (160 nL enrichment column, 140x0.075 mm² i.d. analytical column), both with graphitized carbon as the stationary phase. Both chips offered good sensitivity and reproducibility in separating a heterogeneous mixture of neutral and anionic oligosaccharides between injections. Increasing the length and volume of the enrichment and the analytical columns improved resolution of the peaks. Complex type N-linked oligosaccharides were the most abundant oligosaccharides in human serum accounting for ~96% of the total glycans identified, while hybrid and high mannose type oligosaccharides comprise the remaining ~4%.</description><identifier>ISSN: 1615-9853</identifier><identifier>EISSN: 1615-9861</identifier><identifier>DOI: 10.1002/pmic.200800249</identifier><identifier>PMID: 19288519</identifier><language>eng</language><publisher>Weinheim: Wiley-VCH Verlag</publisher><subject>Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Blood Proteins - chemistry ; Blood Proteins - metabolism ; Chromatography, High Pressure Liquid ; FT‐ICR MS ; Fundamental and applied biological sciences. Psychology ; Glycosylation ; HPLC/Chip‐TOF MS ; Human serum ; Humans ; Mass Spectrometry ; Microchip Analytical Procedures ; Miscellaneous ; N‐linked ; Oligosaccharides ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - metabolism ; Polysaccharides - chemistry ; Polysaccharides - metabolism ; Proteins ; Reproducibility of Results ; Sensitivity and Specificity</subject><ispartof>Proteomics (Weinheim), 2009-04, Vol.9 (7), p.1939-1951</ispartof><rights>Copyright © 2009 WILEY‐VCH Verlag GmbH & Co. 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Therefore, identifying the numerous glycoforms, including isomers, can help elucidate the biological function(s) of particular glycans. A method to assess the diversity of the N-linked oligosaccharides released from human serum without derivatization has been developed using on-line nanoLC and high resolution TOF MS. The N-linked oligosaccharides were analyzed with MALDI FT-ICR MS and microchip LC MS (HPLC-Chip/TOF MS). Two microfluidic chips were employed, the glycan chip (40 nL enrichment column, 43x0.075 mm² i.d. analytical column) and the high capacity chip (160 nL enrichment column, 140x0.075 mm² i.d. analytical column), both with graphitized carbon as the stationary phase. Both chips offered good sensitivity and reproducibility in separating a heterogeneous mixture of neutral and anionic oligosaccharides between injections. Increasing the length and volume of the enrichment and the analytical columns improved resolution of the peaks. Complex type N-linked oligosaccharides were the most abundant oligosaccharides in human serum accounting for ~96% of the total glycans identified, while hybrid and high mannose type oligosaccharides comprise the remaining ~4%.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Blood Proteins - chemistry</subject><subject>Blood Proteins - metabolism</subject><subject>Chromatography, High Pressure Liquid</subject><subject>FT‐ICR MS</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycosylation</subject><subject>HPLC/Chip‐TOF MS</subject><subject>Human serum</subject><subject>Humans</subject><subject>Mass Spectrometry</subject><subject>Microchip Analytical Procedures</subject><subject>Miscellaneous</subject><subject>N‐linked</subject><subject>Oligosaccharides</subject><subject>Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - metabolism</subject><subject>Polysaccharides - chemistry</subject><subject>Polysaccharides - metabolism</subject><subject>Proteins</subject><subject>Reproducibility of Results</subject><subject>Sensitivity and Specificity</subject><issn>1615-9853</issn><issn>1615-9861</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNqFkktv1DAQxyMEog-4cgRf6C2Lx87DviBVKx6VClSCni3HsRODE6d2UpQvxOfEq10t5dSTH_Ob_4w9_yx7BXgDGJN302DVhmDM0qHgT7JTqKDMOavg6XFf0pPsLMafGEPNeP08OwFOGCuBn2Z_boI31mnkDRrlbO81-po7O_7SLercquSI4hwWNS9BR2SCH1C_DLtbHZYBLdGOHept16NJB-NDCimNnL1bbItUn3g5-y7IqV-RH5FEqd9U0aWwVQmwE5Jji2Y76Nyb3LgkNaNBxojipNWcBPQc1hfZMyNd1C8P63l2-_HDj-3n_Prbp6vt5XWuSsZ5zinUmHBKCTUcKGEtA15IXOCi0Yy01GjSqIZBTcuWAqOgFBRt2TS1oZgX9Dx7v9edlmbQrdLjHKQTU7CDDKvw0or_I6PtRefvBamrklU8CVwcBIK_W3ScxWCj0s7JUfsliqoGwuqyfBQkuGCEQ5XAzR5M_xZj0ObYDWCx84DYeUAcPZASXj98wz_8MPQEvD0AMirpTEgzs_HIEaBFBXjH8T33OxlkfaSsuPlytX3YxJt9rpFeyC4k_dvvBAPFyZSMYEb_Aj-N2Kg</recordid><startdate>20090401</startdate><enddate>20090401</enddate><creator>Chu, Caroline S</creator><creator>Niñonuevo, Milady R</creator><creator>Clowers, Brian H</creator><creator>Perkins, Patrick D</creator><creator>An, Hyun Joo</creator><creator>Yin, Hongfeng</creator><creator>Killeen, Kevin</creator><creator>Miyamoto, Suzanne</creator><creator>Grimm, Rudolf</creator><creator>Lebrilla, Carlito B</creator><general>Wiley-VCH Verlag</general><general>WILEY‐VCH Verlag</general><general>Wiley-VCH</general><scope>FBQ</scope><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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090401</creationdate><title>Profile of native N-linked glycan structures from human serum using high performance liquid chromatography on a microfluidic chip and time-of-flight mass spectrometry</title><author>Chu, Caroline S ; Niñonuevo, Milady R ; Clowers, Brian H ; Perkins, Patrick D ; An, Hyun Joo ; Yin, Hongfeng ; Killeen, Kevin ; Miyamoto, Suzanne ; Grimm, Rudolf ; Lebrilla, Carlito B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5899-93170293323f91328d8194a0404be82d3fe2bcb81735d31831cc14d5bb7f30943</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Blood Proteins - chemistry</topic><topic>Blood Proteins - metabolism</topic><topic>Chromatography, High Pressure Liquid</topic><topic>FT‐ICR MS</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycosylation</topic><topic>HPLC/Chip‐TOF MS</topic><topic>Human serum</topic><topic>Humans</topic><topic>Mass Spectrometry</topic><topic>Microchip Analytical Procedures</topic><topic>Miscellaneous</topic><topic>N‐linked</topic><topic>Oligosaccharides</topic><topic>Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - metabolism</topic><topic>Polysaccharides - chemistry</topic><topic>Polysaccharides - metabolism</topic><topic>Proteins</topic><topic>Reproducibility of Results</topic><topic>Sensitivity and Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chu, Caroline S</creatorcontrib><creatorcontrib>Niñonuevo, Milady R</creatorcontrib><creatorcontrib>Clowers, Brian H</creatorcontrib><creatorcontrib>Perkins, Patrick D</creatorcontrib><creatorcontrib>An, Hyun Joo</creatorcontrib><creatorcontrib>Yin, Hongfeng</creatorcontrib><creatorcontrib>Killeen, Kevin</creatorcontrib><creatorcontrib>Miyamoto, Suzanne</creatorcontrib><creatorcontrib>Grimm, Rudolf</creatorcontrib><creatorcontrib>Lebrilla, Carlito B</creatorcontrib><collection>AGRIS</collection><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>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proteomics (Weinheim)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chu, Caroline S</au><au>Niñonuevo, Milady R</au><au>Clowers, Brian H</au><au>Perkins, Patrick D</au><au>An, Hyun Joo</au><au>Yin, Hongfeng</au><au>Killeen, Kevin</au><au>Miyamoto, Suzanne</au><au>Grimm, Rudolf</au><au>Lebrilla, Carlito B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Profile of native N-linked glycan structures from human serum using high performance liquid chromatography on a microfluidic chip and time-of-flight mass spectrometry</atitle><jtitle>Proteomics (Weinheim)</jtitle><addtitle>Proteomics</addtitle><date>2009-04-01</date><risdate>2009</risdate><volume>9</volume><issue>7</issue><spage>1939</spage><epage>1951</epage><pages>1939-1951</pages><issn>1615-9853</issn><eissn>1615-9861</eissn><abstract>Protein glycosylation involves the addition of monosaccharides in a stepwise process requiring no glycan template. 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subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Blood Proteins - chemistry Blood Proteins - metabolism Chromatography, High Pressure Liquid FT‐ICR MS Fundamental and applied biological sciences. Psychology Glycosylation HPLC/Chip‐TOF MS Human serum Humans Mass Spectrometry Microchip Analytical Procedures Miscellaneous N‐linked Oligosaccharides Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - metabolism Polysaccharides - chemistry Polysaccharides - metabolism Proteins Reproducibility of Results Sensitivity and Specificity |
title | Profile of native N-linked glycan structures from human serum using high performance liquid chromatography on a microfluidic chip and time-of-flight mass spectrometry |
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