The presence of N-acetyllactosamine and lactose: beta (1-3)N-acetylglucosaminyltransferase activity in human urine.

Normal human urine was found to contain beta (1-3)N-acetylglucosaminyltransferase catalyzing the transfer of N-acetylglucosamine from UDP-GlcNAc to N-acetyllactosamine and lactose. Lacto-N-tetraose which carries the terminal Gal beta (1-3)GlcNAc structure was a poor acceptor. The product of the transferase reaction with N-acetyllactosamine as acceptor was identified by methylation analysis as GlcNAc beta (1-3)Gal beta (1-4)GlcNAc. The beta-linkage of the GlcNAc in the synthesized trisaccharide was confirmed by the action of the specific beta-N-acetylhexosaminidase. The enzyme requires Mn2+ ions for its activity, shows a broad pH optimum from 7 to 9, and appears to have a molecular weight of about 200,000 as estimated by Sephadex gel filtration.