Enzymatic characterization of CMP-NeuAc:Galβ1-4GlcNAc-R α(2-3)-sialyltransferase from human placenta
| Autor: | Nemansky M, van den Eijnden Dh |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Magnetic Resonance Spectroscopy
Stereochemistry Sialyltransferase Placenta Molecular Sequence Data Biochemistry Substrate Specificity chemistry.chemical_compound Pregnancy Glycosyltransferase medicine Animals Humans Molecular Biology chemistry.chemical_classification biology Glycopeptides Cell Biology Acceptor Sialyltransferases Glycopeptide Rats Sialic acid medicine.anatomical_structure Enzyme Carbohydrate Sequence Liver chemistry biology.protein Cattle Female Protons Glycoprotein |
| Zdroj: | Glycoconjugate Journal. 10:99-108 |
| ISSN: | 1573-4986 0282-0080 |
| DOI: | 10.1007/bf00731193 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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