Uhlenbruck G, Dahr W, Schmalisch R, Janssen E
Blut. 1976 Mar;32(3):163-70. doi: 10.1007/BF00995909.
Results with modified human red cell membrane sialoglycoproteins indicate that alkali-labile sialic acid and amino groups are parts of the erythrocyte receptor sites recognized by common rabbit and human anti-M and -N sera. The "N" antigen, demonstrable in MM glycoprotein preparations by rabbit anti-N, has structural properties which are similar to those of the MN receptors. Sialic acid, amino groups and carbohydrate, susceptible to periodate oxidation, are not involved in the Ss antigen sites. The specificity of the Vicia graminea lectin is dependent on free amino and carboxyl groups. Its affinity for the substances is increased by blocking of amino groups.
对修饰的人红细胞膜唾液糖蛋白的研究结果表明，碱不稳定唾液酸和氨基是普通兔和人抗-M及抗-N血清所识别的红细胞受体位点的组成部分。兔抗-N在MM糖蛋白制剂中可检测到的“N”抗原，其结构特性与MN受体相似。易被高碘酸盐氧化的唾液酸、氨基和碳水化合物不参与Ss抗原位点。蚕豆凝集素的特异性取决于游离氨基和羧基。氨基被封闭后，其对这些物质的亲和力会增加。
