Characterization of Protein N‐Glycosylation
Although mass spectrometry (MS)‐based protein identification is a straightforward task, the characterization of most posttranslational modifications still represents a challenge. N‐glycosylation with its well known consensus sequence, common core structure, and “universally” active endoglycosidase s...
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| Veröffentlicht in: | Methods in Enzymology 2005, Vol.405, p.116-138 |
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| creator | Medzihradszky, Katalin F. |
| description | Although mass spectrometry (MS)‐based protein identification is a straightforward task, the characterization of most posttranslational modifications still represents a challenge. N‐glycosylation with its well known consensus sequence, common core structure, and “universally” active endoglycosidase seems to belong to the easier category. In this chapter, MS methods for the analysis of N‐glycosylated proteins are reviewed. In particular, LC–MS analysis of glycoprotein digests is discussed in detail. The examples included in this chapter illustrate the improved detection sensitivities achieved during the last decade. The characterization of site heterogeneity and of site occupancy is addressed. Low‐energy collision‐induced dissociation (CID) fragmentation of N‐linked glycopeptides and their sodium‐adducts is also described. |
| doi_str_mv | 10.1016/S0076-6879(05)05006-8 |
| format | Article |
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Low‐energy collision‐induced dissociation (CID) fragmentation of N‐linked glycopeptides and their sodium‐adducts is also described.</description><subject>Animals</subject><subject>Chromatography</subject><subject>Chromatography, Liquid</subject><subject>Glycopeptides - chemistry</subject><subject>Glycoside Hydrolases - chemistry</subject><subject>Glycosylation</subject><subject>Humans</subject><subject>Mass Spectrometry - methods</subject><subject>Models, Chemical</subject><subject>Peptides - chemistry</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteins - chemistry</subject><subject>Sodium - chemistry</subject><subject>Spectrometry, Mass, Electrospray Ionization</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods</subject><subject>Time Factors</subject><subject>Ultraviolet Rays</subject><issn>0076-6879</issn><issn>1557-7988</issn><isbn>9780121828103</isbn><isbn>0121828107</isbn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kEtOwzAQhi0eolXpEUBdIVgYZuL4tUKogoKEAAlYW8ZxhFGaFDtFKiuOwBk5CekDZjOL-WY0_0fIAcIpAoqzRwApqFBSHwM_AQ4gqNoifeRcUqmV2iZDLRVghipTCGyH9P9XemSY0ht0xaVkGe6RHoocGUPWJ3T8aqN1rY_h07ahqUdNOXqITetDPbr7-fqeVAvXpEW1Gu6T3dJWyQ83fUCery6fxtf09n5yM764pY4p1tKMaaYh86WWuRQ2L7gU2iKzhcizvARwqhAcJKqclZnTXKBWwLlDpYEJYANytL47i8373KfWTENyvqps7Zt5MkKDBK6xAw834Pxl6gszi2Fq48L8BeyA8zXgu3c_go8mueBr54sQvWtN0QSDYJaWzcqyWSozwM3KslHsFyNbaNs</recordid><startdate>2005</startdate><enddate>2005</enddate><creator>Medzihradszky, Katalin F.</creator><general>Elsevier Science & Technology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>2005</creationdate><title>Characterization of Protein N‐Glycosylation</title><author>Medzihradszky, Katalin F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c383t-2393902ef97476a4d5769a13ad6424f00c8d65071843f2c956198055c18903603</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Animals</topic><topic>Chromatography</topic><topic>Chromatography, Liquid</topic><topic>Glycopeptides - chemistry</topic><topic>Glycoside Hydrolases - chemistry</topic><topic>Glycosylation</topic><topic>Humans</topic><topic>Mass Spectrometry - methods</topic><topic>Models, Chemical</topic><topic>Peptides - chemistry</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteins - chemistry</topic><topic>Sodium - chemistry</topic><topic>Spectrometry, Mass, Electrospray Ionization</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods</topic><topic>Time Factors</topic><topic>Ultraviolet Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Medzihradszky, Katalin F.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Methods in Enzymology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Medzihradszky, Katalin F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of Protein N‐Glycosylation</atitle><jtitle>Methods in Enzymology</jtitle><addtitle>Methods Enzymol</addtitle><date>2005</date><risdate>2005</risdate><volume>405</volume><spage>116</spage><epage>138</epage><pages>116-138</pages><issn>0076-6879</issn><eissn>1557-7988</eissn><isbn>9780121828103</isbn><isbn>0121828107</isbn><abstract>Although mass spectrometry (MS)‐based protein identification is a straightforward task, the characterization of most posttranslational modifications still represents a challenge. 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| ispartof | Methods in Enzymology, 2005, Vol.405, p.116-138 |
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| source | ScienceDirect eBooks; MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Chromatography Chromatography, Liquid Glycopeptides - chemistry Glycoside Hydrolases - chemistry Glycosylation Humans Mass Spectrometry - methods Models, Chemical Peptides - chemistry Protein Processing, Post-Translational Proteins - chemistry Sodium - chemistry Spectrometry, Mass, Electrospray Ionization Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods Time Factors Ultraviolet Rays |
| title | Characterization of Protein N‐Glycosylation |
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