Immunochemical studies on Tn erythrocyte glycoprotein.
Glycoproteins were extracted from membranes of erythrocytes that displayed Tn polyagglutination and were compared chemically and immunologically with glycoproteins of group O, MN cells. Tn glycoprotein had lower than normal NANA : protein and sugar : protein ratios, as revealed by direct analysis and polyacrylamide gel electrophoresis, and displayed slower immunoelectrophoretic mobility than glycoproteins of group O, MN cells. Agglutination of Tn cells by Salvia sclarea lectin was inhibited by Tn glycoprotein but not by O, MN glycoprotein. Tn and MN glycoproteins were equally potent inhibitors of influenza virus HA. Our findings indicate than Tn-specific determinants are part of the glycophorin molecule.[1]References
- Immunochemical studies on Tn erythrocyte glycoprotein. Lee, L.T., Frank, S., de Jongh, D.S., Howe, C. Blood (1981) [Pubmed]
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