Biochemical Genetics of MN

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Abstract
Quantitative hemagglutination studies of the MN-hemizygous (M/-) patient and his family are given together with data on the electrophoretic mobility of their red cells. These results, and those obtained on the cells of a donor of the MU phenotype (MU = M+N-S-s-U+; Mu = M+N-S-s-U-), demonstrate shortcomings in the precursor transferase theory of the biochemical genetics of MN antigens. Another theory is proposed, according to which the effects of the MN genes take place exclusively in the protein part of the glycopeptide. The MN proteins would carry acceptor sites for the antigenic oligosaccharides which are put together by enzymes genetically independent of MN. In M glycoproteins, the acceptor sites are close to each other, in doublets, while in N they are all separate.
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