2.4.1.90	UDP-galactose + N-acetyl-D-glucosamine	synthesis of Galbeta1,4GlcNAc groups in N-linked sugar chains of glycoproteins involved in many physiological functions, e.g. sperm-egg interactions, cell migration, and embryonic development, enzyme expression is highly increased during cycloheximide-induced cell apoptosis in liver carcinoma	
2.4.1.90	UDP-galactose + N-acetylglucosamine	-	
2.4.1.90	UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides	-	
2.4.1.90	UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides	the enzyme facilitates sperm binding to the oocyte zona pellucida	
2.4.1.90	UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides	enzyme participates in the biosynthesis of the oligosaccharide structures of glycoproteins and glycolipids	
2.4.1.90	UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides	the enzyme is involved in the biosynthesis of a variety of carbohydrate structures in glycoproteins and glycolipids	
2.4.1.90	UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides	the enzyme may be involved in the synthesis of poly-N-acetyllactosamine, lacto-N-neotetraose and probably lacto-N-neotetraosylceramide in addition to the formation of the Galbeta1-4GlcNAc group of glycoprotein sugar chains and lactose	
2.4.1.90	UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides	the soluble enzyme form from the luminal fluid of the epididymis is suggested to play a role on sperm maturation	
2.4.1.90	UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides	enzyme functions in the coordinate biosynthesis of complex oligosaccharides, proposed to function in intercellular recognition and/or adhesion	
2.4.1.90	UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides	the enzyme may be involved in the synthesis of plasma glycoproteins by the liver during secretion, and may possibly be required for secretion of these proteins