期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1971
卷号：68
期号：8
页码：1753-1756
DOI：10.1073/pnas.68.8.1753
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
关键词：blood group A ; mucin receptor ; cell-surface antigens
