Determination of glycosylation sites and site-specific heterogeneity in glycoproteins

被引：220

作者：

An, Hyun Joo ^{[1
]}

Froehlich, John W. ^{[1
]}

Lebrilla, Carlito B. ^{[1
,2
]}

机构：

[1] Univ Calif Davis, Dept Chem, Davis, CA 95616 USA

[2] Univ Calif Davis, Dept Biochem & Mol Med, Davis, CA 95616 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2009年 / 13卷 / 04期

关键词：

INFRARED MULTIPHOTON DISSOCIATION; IONIZATION MASS-SPECTROMETRY; LINKED GLYCOPEPTIDE IONS; PROTEIN GLYCOSYLATION; ELECTRON-CAPTURE; N-GLYCOPEPTIDES; STRUCTURAL CHARACTERIZATION; FRAGMENTATION BEHAVIOR; NONSPECIFIC PROTEASES; SELECTIVE DETECTION;

D O I：

10.1016/j.cbpa.2009.07.022

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Glycosylation is one of the most common post-translational modifications (PTMs) of proteins. At least 50% of human proteins are glycosylated with some estimates being as high as 70%. Glycoprotein analysis requires determining both the sites of glycosylation as well as the glycan structures associated with each site. Recent advances have led to the development of new analytical methods that employ mass spectrometry extensively making it possible to obtain the glycosylation site and the site microheterogeneity. These tools will be important for the eventual development of glycoproteomics.

引用

收藏

页码：421 / 426

页数：6

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