INVESTIGATION BY 360-MHZ H-1-NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY AND METHYLATION ANALYSIS OF THE SINGLE GLYCAN CHAIN OF CHICKEN OVOTRANSFERRIN

被引：88

作者：

DORLAND, L

HAVERKAMP, J

VLIEGENTHART, JFG

SPIK, G

FOURNET, B

MONTREUIL, J

机构：

[1] UNIV SCI & TECH LILLE I,CNRS,LAB 217,F-59650 VILLENEUVE D ASCQ,FRANCE

[2] FOM,INST ATOOM & MOLECUULFYS,AMSTERDAM,NETHERLANDS

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1979年 / 100卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1979.tb04203.x

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 primary structure of two glycopeptides obtained by pronase digestion of chicken ovotransferrin has been investigated by 360‐MHz proton nuclear magnetic resonance (NMR) spectroscopy and methylation analysis. The two glycopeptides differ in amino acid composition but contain the same carbohydrate moiety, viz: (Formula Presented.) Using the NMR data of some reference compounds the chemical shifts of the anomeric protons and mannose H‐2 protons could be predicted with an accuracy of 0.01 ppm. Copyright © 1979, Wiley Blackwell. All rights reserved

引用

页码：569 / 574

页数：6

共 36 条

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[3]

CHERON A, COMMUNICATION

[4] STRUCTURE OF ASIALO-CARBOHYDRATE UNITS OF HUMAN SEROTRANSFERRIN AS PROVEN BY 360 MHZ PROTON MAGNETIC-RESONANCE SPECTROSCOPY [J].