Modifications of N-acetylneuraminic acid and their influence on the antigen activity of erythrocyte glycoproteins.
作者： Werner Ebert , Jurgen Metz , Dieter Roelcke
DOI: 10.1111/J.1432-1033.1972.TB01862.X
关键词: N-Acetylneuraminic acid 、 Chemistry 、 Periodic acid 、 Glycoprotein 、 Antigen 、 Lysine 、 Biochemistry 、 Neuraminic acid 、 Antigenicity 、 Epitope
摘要: The erythrocyte glycoprotein-bound N-acetylneuraminic acid which determines the blood groups MN and autoantigens Pr1/Pr2 was modified investigated with regard to antigen activities. We confirmed results of Lisowska Morawiecki, who inactivated antigenicity by acetylating 6-amino group lysine glycoproteins, suggesting that electrostatic interactions between carboxyl side-chain lysyl amino ensure stable antigens. Further support for this concept provided our observation amidation also abolished antigenicity. A further differentiation Pr1 Pr2 elucidated oxidation polyhydroxy side chains acid.
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