STRUCTURAL-ANALYSIS OF GLYCOPEPTIDES BY POLYACRYLAMIDE-GEL ELECTROPHORESIS

被引：13

作者：

PORETZ, RD ^{[1
]}

PIECZENIK, G ^{[1
]}

机构：

[1] RUTGERS STATE UNIV, BUR BIOL RES, NEW BRUNSWICK, NJ 08903 USA

来源：

ANALYTICAL BIOCHEMISTRY | 1981年 / 115卷 / 01期

关键词：

D O I：

10.1016/0003-2697(81)90541-8

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The use of polyacrylamide gel electrophoresis to resolve fluorescein-derivatized asialoglycopeptides is described. Specific exoglycosidase digestion of pronase glycopeptides of [bovine] fetuin generates a series of degradation products that are resolved by polyacrylamide gel electrophoresis and are visualized by photography. The logarithm of the relative electrophoretic mobility of each degraded glycopeptide is linearly correlated to the number of monosaccharide residues sequentially removed by exoglycosidases. Such an approach allows the quantitative evaluation of the number of saccharide moieties removed by each enzyme at a detection sensitivity of < 20 pmol of each compound. Use of specific endoglycosidases results in direct sizing of oligosaccharide chains.

引用

页码：170 / 176

页数：7

共 14 条

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