CHARACTERIZATION OF OLIGOSACCHARIDES FROM A GLYCOPROTEIN VARIANT OF HUMAN SERUM-ALBUMIN (ALBUMIN CASEBROOK) USING HIGH-PERFORMANCE ANION-EXCHANGE CHROMATOGRAPHY AND NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY

被引：15

作者：

HAYNES, PA ^{[1
]}

BATLEY, M ^{[1
]}

PEACH, RJ ^{[1
]}

BRENNAN, SO ^{[1
]}

REDMOND, JW ^{[1
]}

机构：

[1] CHRISTCHURCH SCH MED, DEPT PATHOL, MOLEC PATHOL LAB, CHRISTCHURCH, NEW ZEALAND

来源：

JOURNAL OF CHROMATOGRAPHY-BIOMEDICAL APPLICATIONS | 1992年 / 581卷 / 02期

关键词：

D O I：

10.1016/0378-4347(92)80271-Q

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

The characterisation of oligosaccharides present on albumin Casebrook, a glycoprotein variant of human serum albumin, which contains an N-linked oligosaccharide at an attachment site formed by a point mutation of 494 Asp-->Asn, is described. The monosaccharide compositional analysis of purified glycopeptides suggested the presence of complex biantennary carbohydrate structures. The oligosaccharides which were released by N-glycosidase-F appeared to be a single molecular species according to their retention on high-performance anion-exchange chromatography. The structure of the oligosaccharide was suggested by sequential exoglycosidase digestions and confirmed by proton nuclear magnetic resonance spectroscopy. It was concluded that the oligosaccharides were essentially homogeneous and consisted of an alpha(2-6)-disialylated complex biantennary glycan.

引用

页码：187 / 193

页数：7

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