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Mass Spectrom Rev. 2015 Mar-Apr;34(2):148-65. doi: 10.1002/mas.21428. Epub 2014 Jun 2.

Quantitative mass spectrometric analysis of glycoproteins combined with enrichment methods.

Author information

1
Division of Mass Spectrometry, Korea Basic Science Institute, Cheongwon-Gun, 363-883, Republic of Korea.

Abstract

Mass spectrometry (MS) has been a core technology for high sensitive and high-throughput analysis of the enriched glycoproteome in aspects of quantitative assays as well as qualitative profiling of glycoproteins. Because it has been widely recognized that aberrant glycosylation in a glycoprotein may involve in progression of a certain disease, the development of efficient analysis tool for the aberrant glycoproteins is very important for deep understanding about pathological function of the glycoprotein and new biomarker development. This review first describes the protein glycosylation-targeting enrichment technologies mainly employing solid-phase extraction methods such as hydrizide-capturing, lectin-specific capturing, and affinity separation techniques based on porous graphitized carbon, hydrophilic interaction chromatography, or immobilized boronic acid. Second, MS-based quantitative analysis strategies coupled with the protein glycosylation-targeting enrichment technologies, by using a label-free MS, stable isotope-labeling, or targeted multiple reaction monitoring (MRM) MS, are summarized with recent published studies.

KEYWORDS:

affinity enrichment; hydrazide; lectin; multiple reaction monitoring; protein glycosylation; quantitative mass spectrometry; stable isotope labeling

PMID:
24889823
PMCID:
PMC4340049
DOI:
10.1002/mas.21428
[Indexed for MEDLINE]
Free PMC Article

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