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胎球蛋白糖蛋白中天冬酰胺连接寡糖的结构,其中唾液酸连接到N-乙酰葡糖胺上。

Structures of asparagine-linked oligosaccharides of the glycoprotein fetuin having sialic acid linked to N-acetylglucosamine.

作者信息

Cumming D A, Hellerqvist C G, Harris-Brandts M, Michnick S W, Carver J P, Bendiak B

机构信息

Department of Medical Genetics, University of Toronto, Ontario, Canada.

出版信息

Biochemistry. 1989 Jul 25;28(15):6500-12. doi: 10.1021/bi00441a051.

DOI:10.1021/bi00441a051
PMID:2477057
Abstract

In the accompanying paper (Bendiak et al., 1989), the separation of a series of oligosaccharides released from asparagine residues of fetuin was described. A series of NMR experiments, which included one- and two-dimensional nuclear Overhauser enhancement, two-dimensional correlation spectroscopy, and two-dimensional relayed-coherence spectroscopy, as well as permethylation analyses, established a Gal beta 1----3(NeuAc alpha 2----6)GlcNAc beta 1----4Man unit common to a series of purified structures. These oligosaccharides contained either three, four, or five glycosidically linked sialic acid residues. The NeuAc residue in alpha 2----6 linkage to GlcNAc gives rise to diagnostic chemical shift perturbations of particular proton signals in the oligosaccharides.

摘要

在随附论文(本迪亚克等人,1989年)中,描述了从胎球蛋白天冬酰胺残基释放的一系列寡糖的分离过程。一系列核磁共振实验,包括一维和二维核Overhauser增强、二维相关光谱和二维接力相干光谱,以及全甲基化分析,确定了一系列纯化结构共有的Galβ1----3(NeuAcα2----6)GlcNAcβ1----4Man单元。这些寡糖含有三个、四个或五个糖苷键连接的唾液酸残基。与GlcNAc以α2----6键连接的NeuAc残基会导致寡糖中特定质子信号出现诊断性化学位移扰动。

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1
Structures of asparagine-linked oligosaccharides of the glycoprotein fetuin having sialic acid linked to N-acetylglucosamine.胎球蛋白糖蛋白中天冬酰胺连接寡糖的结构,其中唾液酸连接到N-乙酰葡糖胺上。
Biochemistry. 1989 Jul 25;28(15):6500-12. doi: 10.1021/bi00441a051.
2
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J Biol Chem. 1988 Jun 25;263(18):8677-84.

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