The β1,6-GlcNAc transferase activity present in hog gastric mucosal microsomes catalyses site-specific branch formation on a long polylactosamine backbone
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(97)00818-1/fullpdf
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4. Structure of branched lactosaminoglycan, the carbohydrate moiety of band 3 isolated from adult human erythrocytes.
5. Structural characterization of the asparagine-linked oligosaccharides from Trypanosoma brucei type II and type III variant surface glycoproteins.
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1. Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update covering the period 1999–2000;Mass Spectrometry Reviews;2006
2. Purification and cDNA cloning of UDP-GlcNAc:GlcNAcbeta1-3Galbeta1-4Glc(NAc)-R [GlcNAc to Gal]beta1,6N-acetylglucosaminyltransferase from rat small intestine: a major carrier of dIGnT activity in rat small intestine;Glycobiology;2003-01-22
3. Several polylactosamine-modifying glycosyltransferases also use internal GalNAc 1-4GlcNAc units of synthetic saccharides as acceptors;Glycobiology;2002-03-01
4. Biosynthesis and Function of ß 1,6 Branched Mucin-Type Glycans;The Molecular Immunology of Complex Carbohydrates —2;2001
5. Polyglycosylceramides, Poly-N-acetyllactosamine-Containing Glycosphingolipids: Methods of Analysis, Structure, and Presumable Biological Functions;Chemical Reviews;2000-11-10
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