IDENTIFICATION AND STRUCTURAL CHARACTERIZATION OF A MANNOSE-6-PHOSPHATE CONTAINING OLIGOMANNOSIDIC N-GLYCAN FROM HUMAN ERYTHROPOIETIN SECRETED BY RECOMBINANT BHK-21-CELLS

被引:33
作者
NIMTZ, M [1 ]
WRAY, V [1 ]
RUDIGER, A [1 ]
CONRADT, HS [1 ]
机构
[1] GESELL BIOTECHNOL FORSCH MBH,DEPT CELL BIOL & GENET,D-38124 BRAUNSCHWEIG,GERMANY
关键词
RECOMBINANT HUMAN ERYTHROPOIETIN; BABY HAMSTER KIDNEY CELLS (BHK-21); PHOSPORYLATED OLIGOMANNOSIDIC GLYCAN; MANNOSE-6-PHOSPHATE; 1- AND 2-D NMR SPECTROSCOPY; LYSOSOMAL RECOGNITION SIGNAL;
D O I
10.1016/0014-5793(95)00473-M
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 sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site. Mass spectrometry and both 1- and 2-dimensional NMR techniques revealed a high mannose type structure (Man(6)) with a phospho-diesterbridged N-acetylglucosamine as follows: [GRAPHICS] and FK-506 binding proteins [Rahfeld et al, (1994) FEES Lett, 352, 180-184]. Should Ptf1p display PPIase activity, it would be the first characterized, eukaryotic member of this putative family, which is essential for growth.
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页码:203 / 208
页数:6
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