Blanchard D, Asseraf A, Prigent M J, Cartron J P
Biochem J. 1983 Aug 1;213(2):399-404. doi: 10.1042/bj2130399.
The membranes from Miltenberger Class I (Mi I) and II (Mi II) erythrocytes, two rare variants at the blood group MNSs locus, exhibited an abnormal glycoprotein of 32 kDa apparent molecular mass sharply stained by the periodic acid/Schiff procedure and a decreased content of glycoprotein alpha (synonym glycophorin A, glycoprotein MN) as seen on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Purified 125I-labelled Vicia graminea lectin binds to the unusual 32 kDa glycoprotein separated from Mi I and Mi II erythrocyte membrane of blood group NN or MN, but no significant labelling of this band was observed with Mi samples typed MM. On the basis of such lectin-labelling experiments we have described two heterozygous MN, Mi I individuals that carry one copy of an M gene producing a normal alpha-glycoprotein with M-specificity and one copy of a MiI gene producing a 32 kDa glycoprotein with N-specificity. Further investigations have shown that the 32 kDa glycoprotein was immunoprecipitated by two mouse monoclonal antibodies (R18 and R10) reacting specifically with the external domain of glycoprotein alpha. These results demonstrate that Mi I and Mi II erythrocytes carry an unusual variant of glycoprotein alpha.
米尔滕贝格尔I类(Mi I)和II类(Mi II)红细胞的膜,血型MNSs位点的两种罕见变异体,显示出一种表观分子量为32 kDa的异常糖蛋白,经高碘酸/席夫氏法染色后颜色很深,且十二烷基硫酸钠/聚丙烯酰胺凝胶电泳显示糖蛋白α(同义词血型糖蛋白A、糖蛋白MN)含量降低。纯化的125I标记的蚕豆凝集素可与从血型NN或MN的Mi I和Mi II红细胞膜中分离出的异常32 kDa糖蛋白结合,但在MM血型的Mi样本中未观察到该条带的明显标记。基于此类凝集素标记实验,我们描述了两个杂合的MN、Mi I个体,它们携带一个产生具有M特异性的正常α-糖蛋白的M基因拷贝和一个产生具有N特异性的32 kDa糖蛋白的MiI基因拷贝。进一步研究表明,32 kDa糖蛋白可被两种与糖蛋白α的外部结构域特异性反应的小鼠单克隆抗体(R18和R10)免疫沉淀。这些结果表明,Mi I和Mi II红细胞携带一种异常的糖蛋白α变体。