β-glucosylation of chitooligomers by galactosyltransferase
Galactosyltransferase from bovine milk was found to be able to utilise UDP-Glc to transfer Glc onto GlcNAc and chitooligomers [-β-GlcNAc-(1 → 4)- ](n), n = 2-4. β-Glucosylated products were used in binding studies with NKR-P1A protein cloned from rat natural killer cells.
Kren, Vladimir,Dvorakova, Jana,Gambert, Ulrike,Sedmera, Petr,Havlicek, Vladimir,Thiem, Joachim,Bezouska, Karel
Enzymatic galactosylation of cello- and chito-oligomers
Terminal galactosylations of cello- and chito-oligomers are studied employing galactosyltransferase with and without α-lactalbumin. The lactose synthase complex allows just for galactosylation of cellobiose in lower yield but not for higher cello-oligomers. In contrast, the affinity in galactosylation of chito-oligomers increases with higher members to reach the maximum at chitohexaose with only a 30% reduction in transfer rate. In addition to kinetic data, preparative studies with a number of acceptor substrates gave galactosylated oligosaccharides in high yields. (Figure Presented). Copyright Taylor & Francis Group, LLC.
Galactosidase-assisted synthesis en route to type I and type II structures of chitooligomers1
Transgalactosylation of chitobiose and chitotriose led to formation of terminally (β1-3)- and (β1-4)-galactosylated chitooligosaccharides ready for fucosylation to give Lewisa and Lewisx motifs. Their structures could be assigned emp
Gambert, Ulrike,Conradt, Harald S.,Nimtz, Manfred,Thiem, Joachim
p. 621 - 629
(2007/10/03)
Synthesis of galactose-terminated oligosaccharides by use of galactosyltransferase
Galactosyltransferase catalyzes the galactosylation of oligosaccharides terminated by glucose and by 2-acetamido-2-deoxy glucopyranose, respectively. Variations concerning the acceptor substrate as well as the donor substrate are described.
Thiem,Wiemann
p. 141 - 145
(2007/10/02)
Kombinierte chemoenzymatische Synthese von N-Glycoproteinbausteinen
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Thiem, Joachim,Wiemann, Torsten
p. 78 - 80
(2007/10/02)
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