STRUCTURAL DETERMINATION OF 2 N-LINKED GLYCANS ISOLATED FROM RECOMBINANT HUMAN LACTOFERRIN EXPRESSED IN BHK CELLS

被引：29

作者：

LEGRAND, D ^{[1
]}

SALMON, V ^{[1
]}

CODDEVILLE, B ^{[1
]}

BENAISSA, M ^{[1
]}

PLANCKE, Y ^{[1
]}

SPIK, G ^{[1
]}

机构：

[1] UNIV SCI & TECH LILLE FLANDRES ARTOIS,CHIM BIOL LAB,CNRS,UMR 111,F-59655 VILLENEUVE DASCQ,FRANCE

来源：

FEBS LETTERS | 1995年 / 365卷 / 01期

关键词：

HUMAN LACTOFERRIN; LACTOTRANSFERRIN; N-GLYCAN; RECOMBINANT GLYCOPROTEIN; BHK CELL;

D O I：

10.1016/0014-5793(95)00441-B

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：

A full-length cDNA coding for human lactoferrin was isolated from a mammary gland library and the recombinant protein was expressed in BHK cells as described by Stowell K.M. et al, [1998, Biochem. J. 276, 349-355]. Two N-linked glycans from purified recombinant lactoferrin were released by hydrazinolysis and analyzed by 400-MHz H-1-NMR spectroscopy. The identified structures corresponded to N-acetyllactosaminic biantennary glycans and were alpha-2,3-disialylated forms (80%) or alpha-2,3-monosialylated (20%) forms. Moreover, 70% of total glycans were alpha-1,6-fucosylated at the GlcNAc residue linked to asparagine, In regard to its glycan moiety, the recombinant glycoprotein is close to native lactoferrins from milk or leucocytes but shows specific structural features which should be taken into account prior to in vivo and in vitro biological studies.

引用

页码：57 / 60

页数：4

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