DC Field | Value | Language |
---|---|---|
dc.contributor.author | Y H Ahn | - |
dc.contributor.author | E S Ji | - |
dc.contributor.author | P M Shin | - |
dc.contributor.author | K H Kim | - |
dc.contributor.author | Yong Sam Kim | - |
dc.contributor.author | Jeong Heon Ko | - |
dc.contributor.author | J S Yoo | - |
dc.date.accessioned | 2017-04-19T09:27:33Z | - |
dc.date.available | 2017-04-19T09:27:33Z | - |
dc.date.issued | 2012 | - |
dc.identifier.issn | 0003-2654 | - |
dc.identifier.uri | 10.1039/c1an15775b | ko |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/10499 | - |
dc.description.abstract | A 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.publisher | Royal Soc Chem | - |
dc.title | A multiplex lectin-channel monitoring method for human serum glycoproteins by quantitative mass spectrometry | - |
dc.title.alternative | A multiplex lectin-channel monitoring method for human serum glycoproteins by quantitative mass spectrometry | - |
dc.type | Article | - |
dc.citation.title | Analyst | - |
dc.citation.number | 3 | - |
dc.citation.endPage | 703 | - |
dc.citation.startPage | 691 | - |
dc.citation.volume | 137 | - |
dc.contributor.affiliatedAuthor | Yong Sam Kim | - |
dc.contributor.affiliatedAuthor | Jeong Heon Ko | - |
dc.contributor.alternativeName | 안영희 | - |
dc.contributor.alternativeName | 지은선 | - |
dc.contributor.alternativeName | 신박민 | - |
dc.contributor.alternativeName | 김광회 | - |
dc.contributor.alternativeName | 김용삼 | - |
dc.contributor.alternativeName | 고정헌 | - |
dc.contributor.alternativeName | 유종신 | - |
dc.identifier.bibliographicCitation | Analyst, vol. 137, no. 3, pp. 691-703 | - |
dc.identifier.doi | 10.1039/c1an15775b | - |
dc.description.journalClass | Y | - |
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