Branching and elongation with lactosaminoglycan chains of N-linked oligosaccharides result in a shift toward termination withα2→3-linked rather than withα2→6-linked sialic acid residues-Reference-Cited by-同舟云学术

Branching and elongation with lactosaminoglycan chains of N-linked oligosaccharides result in a shift toward termination withα2→3-linked rather than withα2→6-linked sialic acid residues

Published:1995-04-24 Issue:3 Volume:363 Page:280-284
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Nemansky Martin,Schiphorst Wietske E.C.M.,Van den Eijnden Dirk H.

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(95)00336-8/fullpdf

Reference35 articles.

1. Primary Structure of Glycoprotein Glycans Basis for the Molecular Biology of Glycoproteins

2. Branch specificity of bovine colostrum CMP-sialic acid: Gal beta 1—4GlcNAc-R alpha 2—6-sialyltransferase. Sialylation of bi-, tri-, and tetraantennary oligosaccharides and glycopeptides of the N-acetyllactosamine type.

3. Enzymatic properties of beta-D-galactoside alpha2 leads to 6 sialytransferase from bovine colostrum.

4. Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Gal beta 1 to 3(4)GlcNAc alpha 2 to 3 sialyltransferase and a Gal beta 1 to 4GlcNAc alpha 2 to 6 sialyltransferase from rat liver.

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