COMPARISON OF THE CARBOHYDRATE MOIETIES OF RECOMBINANT SOLUBLE FC-EPSILON RECEPTOR (SFC-EPSILON-RII/SCD23) EXPRESSED IN SACCHAROMYCES-CEREVISIAE AND CHINESE-HAMSTER OVARY CELLS - DIFFERENT O-GLYCOSYLATION SITES ARE USED BY YEAST AND MAMMALIAN-CELLS

被引：5

作者：

KALSNER, I

SCHNEIDER, FJ

GEYER, R

AHORN, H

MAURERFOGY, I

机构：

[1] UNIV GIESSEN KLINIKUM,INST BIOCHEM,W-6300 GIESSEN,GERMANY

[2] BENDER & CO GES MBH,ERNST BOEHRINGER INST ARZNEIMITTELFORSCH,A-1121 VIENNA,AUSTRIA

来源：

GLYCOCONJUGATE JOURNAL | 1992年 / 9卷 / 04期

关键词：

O-GLYCOSYLATION IN YEAST; O-GLYCOSYLATION IN CHO CELLS; SOLUBLE FC-EPSILON-RII; METHYLATION ANALYSIS; SEQUENTIAL DEGRADATION WITH EXOGLYCOSIDASES;

D O I：

10.1007/BF00731167

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：

Recombinant human soluble low affinity receptor for the Fc portion of IgE (sFc(epsilon)RII/sCD23) was produced in Saccharomyces cerevisiae or Chinese hamster ovary cells and subjected to carbohydrate analysis. Applied methods included analytical SDS-PAGE, reversed phase HPLC, methylation analysis and sequential degradation with exoglycosidases. The results revealed that sFc(epsilon)RII derived from Chinese hamster ovary cells is glycosylated exclusively at Ser-147, containing mainly the trisaccharide Sia(alpha-2-3)Gal(beta-1-3)GalNAc, whereas the yeast derived glycoprotein was glycosylated at Ser-167 and contained only alpha-mannosyl residues. It is shown here for the first time that different amino acids of a given protein can be O-glycosylated when expressed in yeast or Chinese hamster ovary cells.

引用

收藏

页码：209 / 216

页数：8

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