Molecular analysis of a UDP-GlcNAc:polypeptide - N -acetylglucosaminyltransferase implicated in the initiation of mucin-type O -glycosylation in Trypanosoma cruzi

By Heise Norton   Singh Divyendu   van der Wel Hanke   Sassi Slim O   Johnson Jennifer M   Feasley Christa L   Koeller Carolina M   Previato Jose O   Mendona-Previato Lucia   West Christopher M  

Glycobiology, Vol. 19, Iss. 8, 2009-08 ,pp. : 918-933

Oxford University Press

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Identification and characterization of a novel UDP-GalNAc:GlcA-R α1,4- N -acetylgalactosaminyltransferase from a human sarcoma cell line

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Oxford University Press

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Bovine mammary gland UDP-GalNAc:GlcNAc-R 1→4- N -acetylgalactosaminyltransferase is glycoprotein hormone nonspecific and shows interaction with α-lactalbumin

By van den Nieuwenhof I.M.   Schiphorst W.E.C.M.   van Die I.   van den Eijnden D.H.  

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Purification and cDNA cloning of UDP-GlcNAc:GlcNAc1-3Gal1-4Glc(NAc)-R [GlcNAc to Gal]1,6 N -acetylglucosaminyltransferase from rat small intestine: a major carrier of dIGnT activity in rat small intestine

By Renkonen O.  

Glycobiology, Vol. 13, Iss. 5, 2003-05 ,pp. : 387-400

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UDP-GlcNAc concentration is an important factor in the biosynthesis of β 1,6-branched oligosaccharides: regulation based on the kinetic properties of N -acetylglucosaminyltransferase V

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