Previously we reported the occurrence of UDP-GalNAc: Galβ1→4GlcNAc/Glc β-1, 3-
N-acetylgalactosaminyltransferase activity in human plasma. Here, the donor substrate specificity of the enzyme partially purified from blood group O plasma was investigated by means of competition experiments with analogs of donor. The enzyme activity was found to be inhibited most strongly by UDP-GlcNAc among the nucleotide sugars tested, and UDP was the best inhibitor among test nucleotides. UDP-GlcNAc was much more inhibitory than UDP, whereas UDP-GalNAc was much less inhibitory than UDP. These results show that the donor-binding site of enzyme has a high affinity for UDP-GlcNAc, but not UDP-GalNAc, suggesting that the enzyme essentially functions in the transfer of
N-acetylglucosamine. Indeed, UDP-GlcNAc: Galβ1→4GlcNAc/Glc β-1, 3-
N-acetylglucosaminyltransferase activity is known to occur in human plasma. The ratio of
N-acetylgalactosamine to
N-acetylglucosamine transferred to lactose with O or B plasma was 1: 20 when assayed separately at 1 μM of donor, but increased to 1.2: 1 at 5 mM. The nearly identical ratio was obtained with the partially purified enzyme preparation.
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