Structures of asparagine-linked oligosaccharides of the glycoprotein fetuin having sialic acid linked to N-acetylglucosamine
In the accompanying paper (Bendiak et al., 1989), the separation of a series of oligosaccharides released from asparagine residues of fetuin was described. A series of NMR experiments, which included one- and two-dimensional nuclear Overhauser enhancement, two-dimensional correlation spectroscopy, a...
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| Veröffentlicht in: | Biochemistry (Easton) 1989-07, Vol.28 (15), p.6500-6512 |
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| container_title | Biochemistry (Easton) |
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| creator | Cumming, Dale A Hellerqvist, Carl G Harris-Brandts, Marees Michnick, Stephen W Carver, Jeremy P Bendiak, Brad |
| description | In the accompanying paper (Bendiak et al., 1989), the separation of a series of oligosaccharides released from asparagine residues of fetuin was described. A series of NMR experiments, which included one- and two-dimensional nuclear Overhauser enhancement, two-dimensional correlation spectroscopy, and two-dimensional relayed-coherence spectroscopy, as well as permethylation analyses, established a Gal beta 1---3(NeuAc alpha 2---6)GlcNAc beta 1---4Man unit common to a series of purified structures. These oligosaccharides contained either three, four, or five glycosidically linked sialic acid residues. The NeuAc residue in alpha 2---6 linkage to GlcNAc gives rise to diagnostic chemical shift perturbations of particular proton signals in the oligosaccharides. |
| doi_str_mv | 10.1021/bi00441a051 |
| format | Article |
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A series of NMR experiments, which included one- and two-dimensional nuclear Overhauser enhancement, two-dimensional correlation spectroscopy, and two-dimensional relayed-coherence spectroscopy, as well as permethylation analyses, established a Gal beta 1---3(NeuAc alpha 2---6)GlcNAc beta 1---4Man unit common to a series of purified structures. These oligosaccharides contained either three, four, or five glycosidically linked sialic acid residues. The NeuAc residue in alpha 2---6 linkage to GlcNAc gives rise to diagnostic chemical shift perturbations of particular proton signals in the oligosaccharides.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00441a051</identifier><identifier>PMID: 2477057</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Acetylglucosamine ; alpha-Fetoproteins ; Analytical, structural and metabolic biochemistry ; Asialoglycoproteins ; Asparagine ; Biological and medical sciences ; Carbohydrate Conformation ; Carbohydrate Sequence ; Carbohydrates ; Chromatography, Gas ; Fetuins ; Fundamental and applied biological sciences. Psychology ; Glucosamine - analogs & derivatives ; Heterosides ; Magnetic Resonance Spectroscopy ; Methylation ; Molecular Sequence Data ; Oligosaccharides - isolation & purification ; Other biological molecules</subject><ispartof>Biochemistry (Easton), 1989-07, Vol.28 (15), p.6500-6512</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a450t-51f5e41e4e5be81f2de68336c91f27125fe3349f61bb60a1b6e29b341d7ef3eb3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00441a051$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00441a051$$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=19381709$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2477057$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cumming, Dale A</creatorcontrib><creatorcontrib>Hellerqvist, Carl G</creatorcontrib><creatorcontrib>Harris-Brandts, Marees</creatorcontrib><creatorcontrib>Michnick, Stephen W</creatorcontrib><creatorcontrib>Carver, Jeremy P</creatorcontrib><creatorcontrib>Bendiak, Brad</creatorcontrib><title>Structures of asparagine-linked oligosaccharides of the glycoprotein fetuin having sialic acid linked to N-acetylglucosamine</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>In the accompanying paper (Bendiak et al., 1989), the separation of a series of oligosaccharides released from asparagine residues of fetuin was described. A series of NMR experiments, which included one- and two-dimensional nuclear Overhauser enhancement, two-dimensional correlation spectroscopy, and two-dimensional relayed-coherence spectroscopy, as well as permethylation analyses, established a Gal beta 1---3(NeuAc alpha 2---6)GlcNAc beta 1---4Man unit common to a series of purified structures. These oligosaccharides contained either three, four, or five glycosidically linked sialic acid residues. The NeuAc residue in alpha 2---6 linkage to GlcNAc gives rise to diagnostic chemical shift perturbations of particular proton signals in the oligosaccharides.</description><subject>Acetylglucosamine</subject><subject>alpha-Fetoproteins</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Asialoglycoproteins</subject><subject>Asparagine</subject><subject>Biological and medical sciences</subject><subject>Carbohydrate Conformation</subject><subject>Carbohydrate Sequence</subject><subject>Carbohydrates</subject><subject>Chromatography, Gas</subject><subject>Fetuins</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glucosamine - analogs & derivatives</subject><subject>Heterosides</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Methylation</subject><subject>Molecular Sequence Data</subject><subject>Oligosaccharides - isolation & purification</subject><subject>Other biological molecules</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkE1v1DAQhi0EKkvhxBnJF-CAAnZix8mxqigfqgC1BSQu1sQZZ916k8V2ECvx4zFKVDhwmrHeR49HLyGPOXvJWclfdY4xITgwye-QDZclK0Tbyrtkwxiri7Kt2X3yIMbr_BRMiSNyVAqlmFQb8usyhdmkOWCkk6UQ9xBgcCMW3o032NPJu2GKYMwWgusXKm2RDv5gpn2YErqRWkxzHlv44caBRgfeGQrG9XS1pIl-KMBgOvjBzyYLd_mPh-SeBR_x0TqPyeez11enb4vzj2_enZ6cFyAkS4XkVqLgKFB22HBb9lg3VVWbNu-Kl9JiVYnW1rzraga8q7Fsu0rwXqGtsKuOybPFm-_9PmNMeueiQe9hxGmOWrUlb1QjM_hiAU2YYgxo9T64HYSD5kz_6Vr_03Wmn6zaudthf8uu5eb86ZpDNOBtgNG4-FfZVg1XrM1csXAuJvx5m0O40bWqlNRXny71F37x9dvZBdPvM_984cFEfT3NYczl_ffC3-4ApKQ</recordid><startdate>19890725</startdate><enddate>19890725</enddate><creator>Cumming, Dale A</creator><creator>Hellerqvist, Carl G</creator><creator>Harris-Brandts, Marees</creator><creator>Michnick, Stephen W</creator><creator>Carver, Jeremy P</creator><creator>Bendiak, Brad</creator><general>American Chemical Society</general><scope>BSCLL</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>7X8</scope></search><sort><creationdate>19890725</creationdate><title>Structures of asparagine-linked oligosaccharides of the glycoprotein fetuin having sialic acid linked to N-acetylglucosamine</title><author>Cumming, Dale A ; Hellerqvist, Carl G ; Harris-Brandts, Marees ; Michnick, Stephen W ; Carver, Jeremy P ; Bendiak, Brad</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a450t-51f5e41e4e5be81f2de68336c91f27125fe3349f61bb60a1b6e29b341d7ef3eb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Acetylglucosamine</topic><topic>alpha-Fetoproteins</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Asialoglycoproteins</topic><topic>Asparagine</topic><topic>Biological and medical sciences</topic><topic>Carbohydrate Conformation</topic><topic>Carbohydrate Sequence</topic><topic>Carbohydrates</topic><topic>Chromatography, Gas</topic><topic>Fetuins</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glucosamine - analogs & derivatives</topic><topic>Heterosides</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Methylation</topic><topic>Molecular Sequence Data</topic><topic>Oligosaccharides - isolation & purification</topic><topic>Other biological molecules</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cumming, Dale A</creatorcontrib><creatorcontrib>Hellerqvist, Carl G</creatorcontrib><creatorcontrib>Harris-Brandts, Marees</creatorcontrib><creatorcontrib>Michnick, Stephen W</creatorcontrib><creatorcontrib>Carver, Jeremy P</creatorcontrib><creatorcontrib>Bendiak, Brad</creatorcontrib><collection>Istex</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>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cumming, Dale A</au><au>Hellerqvist, Carl G</au><au>Harris-Brandts, Marees</au><au>Michnick, Stephen W</au><au>Carver, Jeremy P</au><au>Bendiak, Brad</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structures of asparagine-linked oligosaccharides of the glycoprotein fetuin having sialic acid linked to N-acetylglucosamine</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1989-07-25</date><risdate>1989</risdate><volume>28</volume><issue>15</issue><spage>6500</spage><epage>6512</epage><pages>6500-6512</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>In the accompanying paper (Bendiak et al., 1989), the separation of a series of oligosaccharides released from asparagine residues of fetuin was described. A series of NMR experiments, which included one- and two-dimensional nuclear Overhauser enhancement, two-dimensional correlation spectroscopy, and two-dimensional relayed-coherence spectroscopy, as well as permethylation analyses, established a Gal beta 1---3(NeuAc alpha 2---6)GlcNAc beta 1---4Man unit common to a series of purified structures. These oligosaccharides contained either three, four, or five glycosidically linked sialic acid residues. The NeuAc residue in alpha 2---6 linkage to GlcNAc gives rise to diagnostic chemical shift perturbations of particular proton signals in the oligosaccharides.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>2477057</pmid><doi>10.1021/bi00441a051</doi><tpages>13</tpages></addata></record> |
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| subjects | Acetylglucosamine alpha-Fetoproteins Analytical, structural and metabolic biochemistry Asialoglycoproteins Asparagine Biological and medical sciences Carbohydrate Conformation Carbohydrate Sequence Carbohydrates Chromatography, Gas Fetuins Fundamental and applied biological sciences. Psychology Glucosamine - analogs & derivatives Heterosides Magnetic Resonance Spectroscopy Methylation Molecular Sequence Data Oligosaccharides - isolation & purification Other biological molecules |
| title | Structures of asparagine-linked oligosaccharides of the glycoprotein fetuin having sialic acid linked to N-acetylglucosamine |
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