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- W2074340246 abstract "1. Various kinds of modification of amino groups of M and N blood group glycoproteins abolished their capacity to inhibit rabbit and human anti-M and anit-N sera. 2. The reversible modification of amino groups revealed that M and N blood group activity was restored after the removal of amino-group-blocking residues. 3. Modification of amino groups had an entirely different effect on the reactivity of red cell glycoproteins with Vicia graminea agglutinin. The serological activity of N glycoprotein towards Vicia graminea anti-N agglutinin was unchanged, whereas the weak activity of M glycoprotein towards this anti-N agglutinin was increased to the level of the of N glycoprotein. 4. These results indicate that there is a structural difference between M and N glycoproteins, which resides beyond the oligosaccharide chains. It suggests in turn that M and N blood group specificity is determined by amino acid sequence in the peptide chains of red cell glycoproteins." @default.
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- W2074340246 date "1975-06-01" @default.
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- W2074340246 title "Modification of Amino Groups of Human-Erythrocyte Glycoproteins and the New Concept on the Structural Basis of M and N Blood-Group Specificity" @default.
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- W2074340246 doi "https://doi.org/10.1111/j.1432-1033.1975.tb04158.x" @default.
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