High-throughput quantitative analysis of plant N-glycan using a DNA sequencer
DC Field | Value | Language |
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dc.contributor.author | Lee, Kyung Jin | - |
dc.contributor.author | Jung, Jin-Hee | - |
dc.contributor.author | Lee, Jung Mi | - |
dc.contributor.author | So, Yangkang | - |
dc.contributor.author | Kwon, Ohsuk | - |
dc.contributor.author | Callewaert, Nico | - |
dc.contributor.author | Kang, Hyun Ah | - |
dc.contributor.author | Ko, Kisung | - |
dc.contributor.author | Oh, Doo-Byoung | - |
dc.date.available | 2019-05-30T03:36:34Z | - |
dc.date.issued | 2009-03 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.issn | 1090-2104 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/23273 | - |
dc.description.abstract | High-throughput quantitative analytical method for plant N-glycan has been developed. All steps, including peptide N-glycosidase (PNGase) A treatment, glycan preparation, and exoglycosidase digestion, were optimized for high-throughput applications using 96-well format procedures and automatic analysis on a DNA sequencer. The glycans of horseradish peroxidase with plant-specific core alpha(1,3)-fucose can be distinguished by the comparison of the glycan profiles obtained via PNGase A and F treatments. The peaks of the glycans with (91%) and without (1.2%) alpha(1,3)-fucose could be readily quantified and shown to harbor bisecting beta(1,2)-xylose via simultaneous treatment with alpha(1,3)-mannosidase and beta(1,2)-xylosidase. This optimized method was successfully applied to analyze N-glycans of plant-expressed recombinant antibody, which was engineered to contain a minor amount of glycan harboring P(1,2)-xylose. These results indicate that our DNA sequencer-based method provides quantitative information for plant-specific N-glycan analysis in a high-throughput manner, which has not previously been achieved by glycan profiling based on mass spectrometry. (c) 2009 Elsevier Inc. All rights reserved. | - |
dc.format.extent | 7 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.title | High-throughput quantitative analysis of plant N-glycan using a DNA sequencer | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/j.bbrc.2009.01.070 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.380, no.2, pp 223 - 229 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.wosid | 000263742200004 | - |
dc.identifier.scopusid | 2-s2.0-60649097908 | - |
dc.citation.endPage | 229 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 223 | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 380 | - |
dc.type.docType | Article | - |
dc.publisher.location | 미국 | - |
dc.subject.keywordAuthor | Plant N-glycan | - |
dc.subject.keywordAuthor | DNA sequencer | - |
dc.subject.keywordAuthor | Glycan analysis | - |
dc.subject.keywordAuthor | alpha(1,3)-Fucose | - |
dc.subject.keywordAuthor | beta(1,2)-Xylose | - |
dc.subject.keywordPlus | LINKED OLIGOSACCHARIDES | - |
dc.subject.keywordPlus | HORSERADISH-PEROXIDASE | - |
dc.subject.keywordPlus | GLYCOSYLATION | - |
dc.subject.keywordPlus | GLYCOPROTEINS | - |
dc.subject.keywordPlus | STRATEGIES | - |
dc.subject.keywordPlus | EQUIPMENT | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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