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Bi-antennary oligo-(N-acetyllactosamino)glycans of I-type are galactosylated preferentially at the GlcNAcβ1-6Gal linked arms by α1,3-galactosyltransferase of bovine thymus

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Abstract

α1,3-Galactosylation of radiolabelled bi-antennary acceptors Galβ1-4GlcNAcβ1-3(Galβ1-4GlcNAcβ1-6)Gal-R (R=1-OH, β1-4GlcNAc or β1-4Glc) with bovine thymus α1,3-galactosyltransferase was studied. At all stages of the reactions the three acceptors reacted faster at the 1 → 6 linked arm than at the 1 → 3 linked branch. Hence, in addition to the doubly α1,3-galactosylated products, practically pure Galβ1-4GlcNAcβ1-3(Galα1-3Galβ1-4GlcNAcβ1-6)Gal-R could be obtained from the three acceptors in reactions that had proceeded to near completion. The isomeric mono-α1,3-galactosylated products were identified by using exoglycosidases to remove the branches unprotected by α1,3-galactoses and by subsequently identifying the resulting linear glycans chromatographically.

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Abbreviations

Gal:

d-galactose

GlcNAc:

N-acetyl-d-glucosamine

Lac:

lactose

LacNAc:

Galβ1-4GlcNAc

MH:

maltoheptaose

MP:

maltopentaose

MT:

maltotriose

MTet:

maltotetraose

WGA:

wheat germ agglutinin

3′:

position 3 of the galactose unit of LacNAc or Lac

6′:

position 6 of the galactose unit of LacNAc or Lac

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Seppo, A., Penttilä, L., Leppänen, A. et al. Bi-antennary oligo-(N-acetyllactosamino)glycans of I-type are galactosylated preferentially at the GlcNAcβ1-6Gal linked arms by α1,3-galactosyltransferase of bovine thymus. Glycoconjugate J 11, 217–225 (1994). https://doi.org/10.1007/BF00731221

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  • DOI: https://doi.org/10.1007/BF00731221

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