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Comparative Study
. 1993 Feb;10(1):99-108.
doi: 10.1007/BF00731193.

Enzymatic characterization of CMP-NeuAc:Gal beta 1-4GlcNAc-R alpha(2-3)-sialyltransferase from human placenta

M Nemansky  1 , D H van den Eijnden
Affiliations
Comparative Study

Enzymatic characterization of CMP-NeuAc:Gal beta 1-4GlcNAc-R alpha(2-3)-sialyltransferase from human placenta

M Nemansky et al. Glycoconj J. 1993 Feb.

Abstract

In this report we present the enzymatic characterization of CMP-NeuAc:Gal beta 1-4GlcNAc-R alpha(2-3)-sialyltransferase from human placenta using placenta membranes as an enzyme preparation. This sialyltransferase is highly sensitive to detergents and prefers type 2 chain (Gal beta 1-4GlcNAc) over type 1 chain (Gal beta 1-3GlcNAc) acceptors. Oligosaccharides and glycopeptides were better acceptor substrates than glycoproteins. Of the branched oligosaccharides, those with a bisected N-acetylglucosamine (GlcNAc) structure appeared to be poorer substrates, while triantennary structures containing a Gal beta 1-4GlcNAc beta 1-4Man alpha 1-3Man branch were preferred. Product characterization, using 400 MHz 1H-NMR spectroscopy, confirmed that sialic acid was introduced into the Gal beta 1-4GlcNAc-R units of the acceptor substrates in an alpha (2-3) linkage, and revealed that this sialyltransferase does not prefer either of the two branches of a complex type di-antennary glycopeptide acceptor for sialic acid attachment. These properties distinguish this enzyme from all other sialyltransferases characterized to date.

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