ISSN:
1573-4986
Keywords:
oligo-N-acetyllactosaminoglycans
;
enzymatic synthesis
;
in vitro
;
GlcNAcβ1-6Galβ1-4GlcNAc/Glc
;
GlcNAcβ1-3(GlcNAcβ1-6)Galβ1-4GlcNAc|Glc
;
GlcNAcβ1-3(GlcNAcβ1-6)Gal
;
kinetics of β-N-acetylhexosaminidase cleavage
;
intramolecular interactions
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract Radiolabelled GlcNAcβ1-3(GlcNAcβ1-6)Gal (1), GlcNAcβ1-3(GlcNAcβ1-6)Galβ1-OCH3 (4), GlcNAcβ1-3(GlcNAcβ1-6)Galβ1-4Glc (7), and GlcNAcβ1-3(GlcNAcβ1-6)Galβ1-4GlcNAc (10) were cleaved partially with jack bean β-N-acetylhexosaminidase (EC 3.2.1.30), and the digests were analysed chromatographically. All four oligosaccharides were hydrolysed faster at the (1-6) branch, than at the (1-3) branch, but a high branch specificity was observed only with the glycan4. The saccharides1 and7 resembled each other in the kinetics of the enzyme-catalysed release of their two non-reducingN-acetylglucosamine units, but the glycan10 was rather different. The partial digestions made it possible to obtain radiolabelled GlcNAcβ1-6Gal, GlcNAcβ1-6Galβ1-OCH3, GlcNAcβ1-6Galβ1-4Glc, and, in particular, GlcNAcβ1-6Galβ1-4GlcNAc.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00731350
Permalink