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- W2108355940 abstract "2-Keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN) was introduced into asialotransferrin and N-acetyllactosamine (LacNAc) from CMP-KDN by using rat liver Galβ1→4GlcNAc α2,6-sialyltransferase to form KDN-transferrin and KDN-LacNAc. These structures contain terminal KDNa2→6Gal-residues, a glycotope that has not yet been described in natural glycoconjugates. KDN was transferred to all four Gal residues in asialotransferrin by this enzyme. The incorporation efficiency of KDN from CMP-KDN into asialotransferrin was about half that of Neu5Ac from CMPNeu5Ac, based on the Vmax/Km values for these donor substrates, 0.0527 min-1 and 0.119 min-1, respectively. The KDNα2→6Gal linkage was resistant to exosialidase treatment, in contrast to the sensitivity of the Neu5Acα2→6Gal linkage. Interestingly, Sambucus sieboldiana agglutinin (SSA) was shown to prefer KDN-transferrin to the corresponding Neu5Ac-transferrin, as estimated by slot-blot analysis. The use of an α2,6-sialyltransferase to synthesize neoglycoproteins containing KDN has not been previously reported. Their facile synthesis using CMP-KDN and sialyltransferases with different specificities offers new possibilities to study the function of neo-KDN-glycoconjugates, and to explore their use in glycotechnology." @default.
- W2108355940 created "2016-06-24" @default.
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- W2108355940 date "1998-03-01" @default.
- W2108355940 modified "2023-10-03" @default.
- W2108355940 title "Synthesis of neoglycoconjugates containing deaminated neuraminic acid (KDN) using rat liver alpha2,6-sialyltransferase" @default.
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- W2108355940 doi "https://doi.org/10.1093/glycob/8.3.277" @default.
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