Spring F A, Judson P A, Daniels G L, Parsons S F, Mallinson G, Anstee D J
Western Regional Blood Transfusion Centre, Southmead, Bristol, London, U.K.
Immunology. 1987 Oct;62(2):307-13.
A new human erythrocyte glycoprotein has been identified by immunoblotting with murine monoclonal antibodies under non-reducing conditions. The glycoprotein has a MW of 70,000 and carries Cromer-related blood group antigens. The monoclonal antibodies also react with normal peripheral blood leucocytes and platelets and several haemopoietic cell lines. The glycoprotein has a reduced MW after sialidase treatment. The MW is markedly reduced in Tn erythrocyte membranes and slightly increased in Cad erythrocyte membranes. These results suggest that the glycoprotein has a substantial content of O-glycans. The glycoprotein appears to be absent from, or grossly altered in, the erythrocytes of two individuals with the rare Inab phenotype.
在非还原条件下，通过用鼠单克隆抗体进行免疫印迹法，鉴定出一种新的人红细胞糖蛋白。该糖蛋白的分子量为70,000，并携带与克罗马血型相关的血型抗原。单克隆抗体还与正常外周血白细胞、血小板以及几种造血细胞系发生反应。经唾液酸酶处理后，该糖蛋白的分子量降低。在Tn红细胞膜中，其分子量显著降低，而在Cad红细胞膜中则略有增加。这些结果表明该糖蛋白含有大量的O-聚糖。在两名具有罕见Inab表型的个体的红细胞中，该糖蛋白似乎缺失或发生了显著改变。
