STRUCTURES OF THE ASPARAGINE-LINKED SUGAR CHAIN OF GLUCOSE TRANSPORTER FROM HUMAN ERYTHROCYTES

被引:19
作者
ENDO, T
KASAHARA, M
KOBATA, A
机构
[1] UNIV TOKYO,INST MED SCI,DEPT BIOCHEM,TOKYO 108,JAPAN
[2] TEIKYO UNIV,SCH MED,BIOPHYS LAB,HACHIOJI,TOKYO 19203,JAPAN
关键词
D O I
10.1021/bi00491a005
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
The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis. They were converted to radioactive oligosaccharides by NaB3H4reduction after N-acetylation and fractionated by anion-exchange column chromatography and Bio-Gel P-4 column chromatography after sialidase treatment. Structural study of each oligosaccharide by exo-and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9·GlcNAc·GlcNAc, and biantennary complex-type oligosaccharides with Manα1→6(±GlcNAcβ1→4)(Manα1→3)Manβ1→ 4GlcNAcβ1→4(±Fucα1→6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains. These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3. © 1990, American Chemical Society. All rights reserved.
引用
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页码:9126 / 9134
页数:9
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