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Titolo:
STABLE EXPRESSION OF THE GOLGI FORM AND SECRETORY VARIANTS OF HUMAN FUCOSYL-TRANSFERASE-III FROM BHK-21-CELLS - PURIFICATION AND CHARACTERIZATION OF AN ENGINEERED TRUNCATED FORM FROM THE CULTURE-MEDIUM
Autore:
COSTA J; GRABENHORST E; NIMTZ M; CONRADT HS;
Indirizzi:
GESELL BIOTECHNOL FORSCH MBH,DEPT PROT GLYCOSYLAT,MASCHERODER WEG 1 D-38124 BRAUNSCHWEIG GERMANY GESELL BIOTECHNOL FORSCH MBH,DEPT PROT GLYCOSYLAT D-38124 BRAUNSCHWEIG GERMANY GESELL BIOTECHNOL FORSCH MBH,DEPT MOL & INSTRUMENTAL STRUCT RES D-38124 BRAUNSCHWEIG GERMANY
Titolo Testata:
The Journal of biological chemistry
fascicolo: 17, volume: 272, anno: 1997,
pagine: 11613 - 11621
SICI:
0021-9258(1997)272:17<11613:SEOTGF>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
GENE ASSOCIATED ALPHA-3/4-FUCOSYL-TRANSFERASE; HAMSTER OVARY CELLS; BETA-TRACE PROTEIN; CARBOHYDRATE STRUCTURES; ACCEPTOR SPECIFICITY; SIALYL-LEX; HUMAN-MILK; OLIGOSACCHARIDES; SELECTIN; ANTIGEN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
J. Costa et al., "STABLE EXPRESSION OF THE GOLGI FORM AND SECRETORY VARIANTS OF HUMAN FUCOSYL-TRANSFERASE-III FROM BHK-21-CELLS - PURIFICATION AND CHARACTERIZATION OF AN ENGINEERED TRUNCATED FORM FROM THE CULTURE-MEDIUM", The Journal of biological chemistry, 272(17), 1997, pp. 11613-11621

Abstract

Stable BHK-21 cell Lines were constructed expressing the Golgi membrane bound form and two secretory forms of the human alpha 1,3/4-fucosyltransferase (amino acids 35-361 and 46-361). It was found that 40% of the enzyme activity synthesized by cells transfected with the Golgi form of the fucosyltransferase was constitutively secreted into the medium. The corresponding enzyme detected by Western blot had an apparent molecular mass similar to those of the truncated secretory forms. The secretory variant (amino acids 46-361) was purified by a single affinity-chromatography step on GDP-Fractogel resin with a 20% final recovery. The purified enzyme had a unique NH2 terminus and contained N-linked endo H sensitive carbohydrate chains at its two glycosylation sites. The fucosyltransferase transferred fucose to the O-4 position of GlcNAc in small oligosaccharides, glycolipids, glycopeptides, and glycoproteins containing the type I Gal beta 1-3GlcNAc motif. The acceptor oligosaccharide in bovine asialofetuin was identified as the Man-3 branched triantennary isomer with one Gal beta 1-3GlcNAc. The type II motif Gal beta 1-4GlcNAc in bi-, tri-, or tetraantennary neutral or alpha 2-3/alpha 2-6 sialylated oligosaccharides with or without N-acetyllactosamine repeats and in native glycoproteins were not modified. The soluble forms of fucosyltransferase III secreted by stably transfected cells may be used for in vitro synthesis of the Lewis(a) determinant on carbohydrates and glycoproteins, whereas Lewis(x) and sialyl-Lewis(x) structures cannot be synthesized.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/06/20 alle ore 23:55:15