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a1>3-GALACTOSYLTRANSFERASE : THE USE OF RECOMBINANT ENZYME FOR THE SYNTHESIS OF a-GALACTOSYLATED GLYCOCONJUGATES
Joziasse, David H. Shaper, Nancy L. Salyer, Linda S. Eijnden, Dirk H. van den Spoel, Aarnoud C. van der Shaper, Joel H.
Joziasse, David H.
Shaper, Nancy L.
Salyer, Linda S.
Eijnden, Dirk H. van den
Spoel, Aarnoud C. van der
Shaper, Joel H.
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Issue Date
1991
Submitted date
2024-02-28
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Abstract
We have reported the isolation and characterization of a bovine cDNA clone containing the complete coding sequence for UDPGal: Galß1>4G1cNAc «1>3-galactosyltransferase (Joziasse, D.H. et al., (1989) J. Biol. Chem. 264, 14290-14297). Insertion of this cDNA clone into the genome of Autographa californica nuclear polyhedrosis virus (AcNPV) and subsequent infection of Sf9 insect cells with recombinant virus, resulted in high-level expression of enzymatically active al>3-galactosyltransferase. The recombinant &1>3-galactosyltransferase could be readily detergent solubilized and subsequently purified by affinity-chromatography on UDP-hexanolamine-Sepharose. The recombinant «1>3-galactosyltransferase showed the expected preference for the acceptor substrate N-acetyllactosamine (GalB1>4G1cNAc), and demonstrated enzyme kinetics identical to those previously reported for affinity-purified calf thymus a1 >3- galactosyltransferase.
Citation
Protein glycosylation, 219 - 220
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Book chapter
conference paper
conference paper
Language
en
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Series/Report no.
GBF monographs ; Volume 15
ISSN
0930-4320
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ISBN
1560811846
3527283676
3527283676
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Attribution-NonCommercial-ShareAlike 4.0 International