Scartezzini P, Forni G L, Baldi M, Izzo C, Sansone G
Br J Haematol. 1982 Aug;51(4):569-76. doi: 10.1111/j.1365-2141.1982.tb02820.x.
We report a study of HEMPAS erythrocyte membrane glycoproteins in relation to proteolytic digestion and surface labelling with galactose-oxidase/NaB[3H]4. The proteolytic digestion of band 3, the major intrinsic glycoprotein of the human erythrocyte membrane, reveals an abnormality in the outer glycosylated segment of this protein. 3H incorporation in band 3 and band 4.5 glycoproteins after treatment with galactose-oxidase/NaB[3H]4 is reduced in HEMPAS red cells suggesting a defective glycosylation of these proteins. These findings together with the persistence of i antigen and the normal presence of I antigen lead us to conclude that erythroblastic membrane features may persist in HEMPAS erythrocytes.
我们报告了一项关于遗传性红细胞生成异常性卟啉病（HEMPAS）红细胞膜糖蛋白与蛋白水解消化及用半乳糖氧化酶/硼氢化钠[3H]4进行表面标记的研究。人红细胞膜的主要内在糖蛋白带3的蛋白水解消化显示该蛋白外糖基化部分存在异常。在HEMPAS红细胞中，用半乳糖氧化酶/硼氢化钠[3H]4处理后，带3和带4.5糖蛋白中3H的掺入减少，提示这些蛋白的糖基化存在缺陷。这些发现连同i抗原的持续存在和I抗原的正常存在使我们得出结论，HEMPAS红细胞中可能存在成红细胞膜特征。
