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.-Reference-Cited by-同舟云学术

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.

Published:1987-02 Issue:5 Volume:262 Page:2025-2033
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Joziasse D.H.,Schiphorst W.E.,Van den Eijnden D.H.,Van Kuik J.A.,Van Halbeek H.,Vliegenthart J.F.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference46 articles.

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2. The Biochemistry of Glycoproteins and Proteoglycans;Kornfeld,1980

3. The identification of terminal α(1→3)-linked galactose in N-acetyllactosamine type of glycopeptides by means of 500-MHz 1H-NMR spectroscopy

4. Characterization of the microheterogeneity in glycoproteins by 500-MHz 1H-NMR spectroscopy of glycopeptide preparations. Application to a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein.

5. Embryonal lactosaminoglycan. The structure of branched lactosaminoglycans with novel disialosyl (sialyl alpha 2—-9 sialyl) terminals isolated from PA1 human embryonal carcinoma cells.

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