Abstract
A novel carbohydrate-rich sialoglycopeptide of apparent molecular mass $$$6 kDa was isolated from the fertilized eggs of Fundulus heteroclitus (euryhaline killi fish). Thisglycopeptide is a member of the L-hyosophorin family, characterized by its high content of carbohydrate (8090% by weight) and formed by depolymerization of the precursor glycopolyprotein (H-hyosophorin) upon fertilization. The structures of the N-glycan chains were unambiguously established by a combination of compositional analysis, methylation analysis, selective chemical degradation (periodate oxidation-Smith degradation and hydrazinolysis-nitrous acid deamination), enzymatic (peptide:N-g]ycosidase F, several β-galactosidases, (β-hexosaminidase and α-galactosidase) digestions and instrumental analyses (1H-NMR and fast atom bombardment mass spectrometry) tohave the novel and unique carbohydrate sequences, Galα1→3(Galβ1→4)Ga1β14GlcNAcβ1→ and Galα1→3(±GalNAcβ1→4GlcNAcβ1→3Galβ1→4)Gal-β1→4GlcNAcβ1→. This study representsthe first detailed investigation of the nature of bulky complex asparagine-linked penta-antennary glycans with a bisecting GlcNAc residue in glycoproteins. Expression of such bulky multiantennaryglycanunits on proteins may be essential during early embryogenesis.
Original language | English |
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Pages (from-to) | 611-624 |
Number of pages | 14 |
Journal | Glycobiology |
Volume | 5 |
Issue number | 6 |
DOIs | |
Publication status | Published - 1995 Sep |
Externally published | Yes |
Keywords
- Carbohydrate-rich sialoglycopeptide
- Hyosophorin
- N-glycans
- Penta-antennary glycans
- α-Gal residue
ASJC Scopus subject areas
- Biochemistry