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. 1971 Aug;68(8):1753–1756. doi: 10.1073/pnas.68.8.1753

N-Acetyl-D-Galactosaminyltransferase in Human Serum and Erythrocyte Membranes

Young S Kim 1,2, Jose Perdomo 1,2, Agustin Bella Jr 1,2, Judith Nordberg 1,2
PMCID: PMC389286  PMID: 5288760

Abstract

This study demonstrates the presence of an N-acetyl-D-galactosaminyltransferase in human serum and in erythrocyte membranes. This enzyme catalyzes the transfer of N-acetyl-D-galactosamine from UDP-N-acetyl-D-galactosamine to a mucin receptor and 2′-fucosyllactose that have blood group H activity and may be responsible, therefore, for blood group A antigenicity. It was present in the serum of individuals with blood group A or AB but was absent from those with blood group B or O. The activity measured in the erythrocyte membrane was low and did not show clear-cut separation among donors of different blood groups. The specificity of this enzyme in serum was suggested by the ability of 2′-fucosyllactose to act as an acceptor, as well as desialyzed porcine submaxillary mucin, while lactose and desialized fetuin failed to accept N-acetyl-D-galactosamine. The catalytic properties of the N-acetyl-D-galactosaminyltransferase from serum and from erythrocyte membranes were similar.

Keywords: blood group A, mucin receptor, cell-surface antigens

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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