PEPTIDE-N(4)-(N-ACETYLGLUCOSAMINYL)ASPARAGINE AMIDASE (PNGASE) ACTIVITY COULD EXPLAIN THE OCCURRENCE OF EXTRACELLULAR XYLOMANNOSIDES IN A PLANT-CELL SUSPENSION

被引：26

作者：

LHERNOULD, S

KARAMANOS, Y

BOURGERIE, S

STRECKER, G

JULIEN, R

MORVAN, H

机构：

[1] UNIV LIMOGES,BIOL CELLULAIRE VEGETALE & VALORISAT ESPECES LIGNEUSES,123 AVE ALBERT THOMAS,F-87060 LIMOGES,FRANCE

[2] CNRS,UNITE MIXTE 111,F-59655 VILLENEUVE DASCQ,FRANCE

[3] UNIV LIMOGES,INST BIOTECHNOL,F-87060 LIMOGES,FRANCE

[4] UNIV SCI & TECH LILLE FLANDRES ARTOIS,CHIM BIOL LAB,F-59655 VILLENEUVE DASCQ,FRANCE

来源：

GLYCOCONJUGATE JOURNAL | 1992年 / 9卷 / 04期

关键词：

XYLOMANNOSIDE; PNGASE; WHITE CAMPION;

D O I：

10.1007/BF00731164

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：

We have previously isolated mannoside and xylomannoside oligosaccharides with one or two terminal reducing N-acetylglucosamine residues from the extracellular medium of white campion (Silene alba) suspension culture. We have now demonstrated the presence of peptide-N4-(N-acetylglucosaminyl)asparagine amidase (PNGase) activity in cell extracts as well in the culture medium that could explain the production of those compounds. An additional xylomannoside, (GlcNAc)Man3(Xyl)GlcNAc(Fuc)GlcNAc, was characterized, and H-1- and C-13-NMR assignments for the oligosaccharide Man3(Xyl)GlcNAc(Fuc)GlcNAc were obtained using homonuclear and heteronuclear spectroscopy (COSY).

引用

页码：191 / 197

页数：7

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