PERMETHYLATION AND TANDEM MASS-SPECTROMETRY OF OLIGOSACCHARIDES HAVING FREE HEXOSAMINE - ANALYSIS OF THE GLYCOINOSITOL PHOSPHOLIPID ANCHOR GLYCAN FROM THE SCRAPIE PRION PROTEIN

被引：57

作者：

BALDWIN, MA

STAHL, N

REINDERS, LG

GIBSON, BW

PRUSINER, SB

BURLINGAME, AL

机构：

[1] UNIV CALIF SAN FRANCISCO,DEPT NEUROL,SAN FRANCISCO,CA 94143

[2] UNIV CALIF SAN FRANCISCO,DEPT BIOCHEM & BIOPHYS,SAN FRANCISCO,CA 94143

[3] UNIV CALIF SAN FRANCISCO,CTR LIVER,SAN FRANCISCO,CA 94143

来源：

ANALYTICAL BIOCHEMISTRY | 1990年 / 191卷 / 01期

关键词：

D O I：

10.1016/0003-2697(90)90405-X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Permethylation of the glycan isolated from the glycoinositol phospholipid (GPI) anchor of the scrapie prion protein (PrPSc) trimethylates a free hexosamine to form a quarternary ammonium salt, substantially increasing the sensitivity for analysis by mass spectrometry. This derivatization induces specific fragmentation reactions in collision-induced dissociation spectra obtained on a four-sector tandem mass spectrometer, identifying the branching pattern of the PrPSc GPI glycan. © 1990.

引用

页码：174 / 182

页数：9

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