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Synthesis of pentasaccharide analogues of theN-glycan substrates ofN-acetylglucosaminyltransferases III, IV and V using tetrasaccharide precursors and recombinantβ-(1 → 2)-N-acetylglucosaminyltransferase II

Authors
Journal
Carbohydrate Research
0008-6215
Publisher
Elsevier
Publication Date
Volume
275
Issue
2
Identifiers
DOI: 10.1016/0008-6215(95)00091-7
Keywords
  • Pentasaccharide Analogues
  • N-Glycan Substrates
  • N-Acetylglucosaminyltransferases
  • β-(1 → 2)-N-Acetylglucosaminyltransferase Ii
Disciplines
  • Biology

Abstract

Abstract Recombinant human UDP-GlcNAc: α-Man-(1 → 6)R β-(1 → 2)- N-acetylglucosaminyltransferase II (EC 2.4.1.143, GlcNAc-T II) was produced in the Sf9 insect cell/baculovirus expression system as a fusion protein with a (His) 6 tag and partially purified by affinity chromatography on a metal chelating column. The partially purified enzyme was used to catalyze the transfer of GlcNAc from UDP-GlcNAc to R- α-Man(1 → 6)( β-GlcNAc(1 → 2) α-Man(1 → 3)) β-Man- O-octyl to form β-GlcNAc(1 → 2)R- α-Man(1 → 6)( β-GlcNAc(1 → 2) α-Man(1 → 3)) β-Man- O-octyl where there is either no modification of the α-Man(1 → 6) residue (7), or where R is 3-deoxy (8), 4-deoxy (9) or 6-deoxy (10). The yields ranged from 64–80%. Products were characterized by 1H and 13C nuclear magnetic resonance spectroscopy and fast atom bombardment mass spectrometry. Compounds 7–10 are pentasaccharide analogues of the biantennary N-glycan substrates of N-acetylglucosaminyltransferases III, IV and V.

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