Duk M, Wu A M, Lisowska E
Department of Immunochemistry, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław.
Glycoconj J. 1994 Aug;11(4):371-4. doi: 10.1007/BF00731211.
Earlier studies showed that Moluccella laevis lectin, which has anti-Tn specificity, reacts more strongly with native or desialylated blood group N glycophorin A than with the respective glycophorins of blood group M. We now present results indicating that Vicia villosa B4 anti-Tn lectin, which does not show detectable reaction with untreated glycophorins or erythrocytes, reacts better with desialylated blood group N antigen than with asialo M antigen. This was demonstrated by three assays: (1) agglutination of asialoerythrocytes; (2) binding of biotinylated lectin to asialoerythrocytes immobilized on ELISA plates; and (3) inhibition of lectin binding to asialo-agalactoglycophorin with asialoglycophorins M and N. These results supply further support for the conclusion that glycophorin of blood group N has more GalNAc residues unsubstituted with Gal (Tn receptors) than glycophorin of blood group M.
早期研究表明，具有抗Tn特异性的光滑罗勒凝集素与天然或去唾液酸化的血型N糖蛋白A的反应比与血型M的相应糖蛋白的反应更强。我们现在展示的结果表明，野豌豆B4抗Tn凝集素与未处理的糖蛋白或红细胞无明显反应，但与去唾液酸化的血型N抗原的反应比与去唾液酸化的M抗原的反应更好。这通过三种测定得以证明：（1）去唾液酸红细胞的凝集；（2）生物素化凝集素与固定在ELISA板上的去唾液酸红细胞的结合；（3）用去唾液酸糖蛋白M和N抑制凝集素与去唾液酸 - 半乳糖凝集素的结合。这些结果进一步支持了以下结论：血型N的糖蛋白比血型M的糖蛋白具有更多未被半乳糖取代的N-乙酰半乳糖胺残基（Tn受体）。
