A multiplex lectin-channel monitoring method for human serum glycoproteins by quantitative mass spectrometry

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dc.contributor.authorY H Ahn-
dc.contributor.authorE S Ji-
dc.contributor.authorP M Shin-
dc.contributor.authorK H Kim-
dc.contributor.authorYong Sam Kim-
dc.contributor.authorJeong Heon Ko-
dc.contributor.authorJ S Yoo-
dc.date.accessioned2017-04-19T09:27:33Z-
dc.date.available2017-04-19T09:27:33Z-
dc.date.issued2012-
dc.identifier.issn0003-2654-
dc.identifier.uri10.1039/c1an15775bko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/10499-
dc.description.abstractA mass profiling method and multiple reaction monitoring (MRM)-based quantitative approach were used to analyze multiple lectin-captured fractions of human serum using different lectins such as aleuria aurantia lectin (AAL), phytohemagglutinin-L 4 (L-PHA), concanavalin A (Con A), and Datura stramonium agglutinin (DSA) to quantitatively monitor protein glycosylation diversity. Each fraction, prepared by multiple lectin-fractionation and tryptic digestion, was analyzed by 1-D LC-MS/MS. Semi-quantitative profiling showed that the list of glycoproteins identified from each lectin-captured fraction is significantly different according to the used lectin. Thus, it was confirmed that the multiplex lectin-channel monitoring (LCM) using multiple lectins is useful for investigating protein glycosylation diversity in a proteome sample. Based on the semi-quantitative mass profiling, target proteins showing lectin-specificity among each lectin-captured fraction were selected and analyzed by the MRM-based method in triplicate using each lectin-captured fraction (average CV 7.9%). The MRM-based analysis for each lectin-captured fraction was similar to those obtained by the profiling experiments. The abundance of each target protein measured varied dramatically, based on the lectin-specificity. The multiplex LCM approach using MRM-based analyses is useful for quantitatively monitoring target protein glycoforms selectively fractionated by multiple lectins. Thus through multiplex LCM rather than single, we could inquire minutely into protein glycosylation states.-
dc.publisherRoyal Soc Chem-
dc.titleA multiplex lectin-channel monitoring method for human serum glycoproteins by quantitative mass spectrometry-
dc.title.alternativeA multiplex lectin-channel monitoring method for human serum glycoproteins by quantitative mass spectrometry-
dc.typeArticle-
dc.citation.titleAnalyst-
dc.citation.number3-
dc.citation.endPage703-
dc.citation.startPage691-
dc.citation.volume137-
dc.contributor.affiliatedAuthorYong Sam Kim-
dc.contributor.affiliatedAuthorJeong Heon Ko-
dc.contributor.alternativeName안영희-
dc.contributor.alternativeName지은선-
dc.contributor.alternativeName신박민-
dc.contributor.alternativeName김광회-
dc.contributor.alternativeName김용삼-
dc.contributor.alternativeName고정헌-
dc.contributor.alternativeName유종신-
dc.identifier.bibliographicCitationAnalyst, vol. 137, no. 3, pp. 691-703-
dc.identifier.doi10.1039/c1an15775b-
dc.description.journalClassY-
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Synthetic Biology and Bioengineering Research Institute > Genome Editing Research Center > 1. Journal Articles
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