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Titolo:
Structural study on the carbohydrate moiety of calf intestinal alkaline phosphatase
Autore:
Bublitz, R; Hoppe, H; Cumme, GA; Thiele, M; Attey, A; Horn, A;
Indirizzi:
Univ Jena, Fac Med, Inst Biochem, D-07743 Jena, Germany Univ Jena Jena Germany D-07743 Med, Inst Biochem, D-07743 Jena, Germany Micromass UK Ltd, Manchester M23 9LZ, Lancs, England Micromass UK Ltd Manchester Lancs England M23 9LZ M23 9LZ, Lancs, England
Titolo Testata:
JOURNAL OF MASS SPECTROMETRY
fascicolo: 8, volume: 36, anno: 2001,
pagine: 960 - 972
SICI:
1076-5174(200108)36:8<960:SSOTCM>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
IONIZATION MASS-SPECTROMETRY; BRUSH-BORDER MEMBRANE; TIME-OF-FLIGHT; LINKED OLIGOSACCHARIDES; N-GLYCOSYLATION; EXOGLYCOSIDASE DIGESTION; PROTEIN GLYCOSYLATION; CELL-CYCLE; GENE; HETEROGENEITY;
Keywords:
tryptic peptides; glycan structures; exoglycosidase digestion; matrix-assisted laser desorption/ionization mass; spectrometry; electrospray ionization mass spectrometry;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Horn, A Univ Jena, Fac Med, Inst Biochem, Nonnenplan 2, D-07743 Jena, Germany Univ Jena Nonnenplan 2 Jena Germany D-07743 D-07743 Jena, Germany
Citazione:
R. Bublitz et al., "Structural study on the carbohydrate moiety of calf intestinal alkaline phosphatase", J MASS SPEC, 36(8), 2001, pp. 960-972

Abstract

Surprisingly alkaline phosphatase (AP) (EC 3.1.3.1) of calf intestine is found in large amounts, e.g. 80%, within chyme. Most of the enzyme is present as a mixture of four differently hydrophobic anchor-bearing forms and only the minor part is present as an anchorless enzyme. To investigate whetherchanges in the N-glycosylation pattern are signals responsible for large-scale liberation from mucosa into chyme, the glycans of the two potential glycosylation sites predicted from cDNA were investigated by matrix-assisted laser desorption/ionization and electrospray ionization mass spectrometry in combination with exoglycosidase treatment after Cryptic digestion and reversed-phase chromatography. The glycans linked to Asn249 are at least eightdifferent, mainly non-fucosylated, biantennary or triantennary structures with a bisecting N-acetylglucosamine. For the most abundant glycopeptide (40%) the following glycan structure is proposed:[GRAPHICS]The glycans linked to Asn410 are a mixture of at least nine, mainly tetraantennary, fucosylated structures with a bisecting N-acetylglucosamine. For the most abundant glycopeptide (35%) the following glycan structure is. proposed:[GRAPHICS]For the structures the linkage data were deduced from the reported specificities of the exoglycosidases used and the specificities of the transglycosidases active in biosynthesis. The majority of glycans are capped by alpha -galactose residues at their non-reducing termini. In contrast to the glycans linked to other AP isoenzymes, no sialylation was observed. Glycopeptide'mass fingerprints' of both glycosylation sites and glycan contents do notdiffer between AP from mucosa and chyme. These results suggest that the observed large-scale liberation of vesicle-bound glycosylphosphatidylinositol(GPI)-anchored AP from mucosa into chyme is unlikely to be mediated by alteration of glycan structures of the AP investigated. Rather, the exocytoticvesicle formation seems to be mediated by the controlled organization of the raft structures embedding GPI-AP. Copyright (C) 2001 John Wiley & Sons, Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 19:35:39