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Resin-Assisted Enrichment of N-Terminal Peptides for Characterizing Proteolytic Processing

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dc.contributor.authorKim, Jong-Seo-
dc.contributor.authorDai, Ziyu-
dc.contributor.authorAryal, Uma K.-
dc.contributor.authorMoore, Ronald J.-
dc.contributor.authorCamp, David G., II-
dc.contributor.authorBaker, Scott E.-
dc.contributor.authorSmith, Richard D.-
dc.contributor.authorQian, Wei-Jun-
dc.date.accessioned2024-05-14T06:48:58Z-
dc.date.available2024-05-14T06:48:58Z-
dc.date.created2023-06-26-
dc.date.issued2013-07-
dc.identifier.citationAnalytical Chemistry, Vol.85 No.14, pp.6826-6832-
dc.identifier.issn0003-2700-
dc.identifier.urihttps://hdl.handle.net/10371/201895-
dc.description.abstractA resin-assisted enrichment method has been developed for specific isolation of protein N-terminal peptides to facilitate LC-MS/MS characterization of proteolytic processing, a major form of posttranslational modifications. In this method, protein thiols are blocked by reduction and alkylation, and protein lysine residues are converted to homoarginines. Protein N-termini are selectively converted to reactive thiol groups, and the thiol-containing N-terminal peptides are then captured by a thiol-affinity resin with high specificity (>97%). The efficiencies of these sequential reactions were demonstrated to be nearly quantitative. The resin-assisted N-terminal peptide enrichment approach was initially applied to a cell lysate of the filamentous fungus Aspergillus niger. Subsequent C-MS/MS analyses resulted in the identification of 1672 unique protein N-termini or proteolytic cleavage sites from 690 unique proteins.-
dc.language영어-
dc.publisherAmerican Chemical Society-
dc.titleResin-Assisted Enrichment of N-Terminal Peptides for Characterizing Proteolytic Processing-
dc.typeArticle-
dc.identifier.doi10.1021/ac401000q-
dc.citation.journaltitleAnalytical Chemistry-
dc.identifier.wosid000322059600040-
dc.identifier.scopusid2-s2.0-84880519251-
dc.citation.endpage6832-
dc.citation.number14-
dc.citation.startpage6826-
dc.citation.volume85-
dc.description.isOpenAccessY-
dc.contributor.affiliatedAuthorKim, Jong-Seo-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.subject.keywordPlusTANDEM MASS-SPECTRA-
dc.subject.keywordPlusSYSTEMATIC IDENTIFICATION-
dc.subject.keywordPlusPOSITIONAL PROTEOMICS-
dc.subject.keywordPlusCLEAVAGE SITES-
dc.subject.keywordPlusPROTEIN-
dc.subject.keywordPlusDERIVATIZATION-
dc.subject.keywordPlusTHROUGHPUT-
dc.subject.keywordPlusSTRATEGY-
dc.subject.keywordPlusSIGNALP-
dc.subject.keywordPlusSCALE-
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  • College of Natural Sciences
  • School of Biological Sciences
Research Area Molecular Interactomics, Proteomics, Systems Biology, 단백체학, 분자상호작용체학, 시스템생물학

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