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  • Title: Bovine colostrum CMP-NeuAc:Gal beta(1-->4)GlcNAc-R alpha(2-->6)-sialyltransferase is involved in the synthesis of the terminal NeuAc alpha(2-->6)GalNAc beta(1-->4)GlcNAc sequence occurring on N-linked glycans of bovine milk glycoproteins.
    Author: Nemansky M, Van den Eijnden DH.
    Journal: Biochem J; 1992 Oct 01; 287 ( Pt 1)(Pt 1):311-6. PubMed ID: 1417784.
    Abstract:
    Bovine colostrum CMP-NeuAc:Gal beta(-->4)GlcNAc-R alpha(2-->6)-sialyltransferase (alpha 6-sialyltransferase) appears to be capable of catalysing alpha 6-sialylation of the disaccharide GalNAc beta(1-->4)GlcNAc to yield the trisaccharide NeuAc alpha(2-->6)GalNAc beta(1-->4)GlcNAc. This provides an enzymic basis for the occurrence of this sialylated structure on the N-linked glycans of a number of bovine milk glycoproteins. Competition experiments using Gal beta(1-->4)GlcNAc and GalNAc beta(-->4)GlcNAc as acceptors indicate that both substrates are recognized by a single active site on the alpha 6-sialyltransferase. Extrapolation of these results suggests that the NeuAc alpha(2-->6)GalNAc beta(1-->4)GlcNAc structural element occurring on the N-linked glycans of several human glycoproteins are similarly synthesized by the action of a Gal beta(1-->4)GlcNAc-R alpha(2-->6)-sialyltransferase.
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