Localization of globoside and Forssman glycolipids on erythrocyte membranes.
Localization of globoside and Forssman glycolipids on erythrocyte membranes.
复制标题
球苷和福斯曼糖脂在红细胞膜上的定位。
DOI：
10.1016/0005-2736(83)90086-x
复制
发表时间：
1983
期刊：
影响因子：
--
通讯作者：
YoungJr,WW
中科院分区：
文献类型：
--
作者：
Tillack,TW;Allietta,M;Moran,RE;YoungJr,WW
使用冷冻蚀刻技术，使用铁蛋白和胶体金作为针对这些糖脂制备的兔抗体的形态学标记，评估了球苷（人红细胞中的主要糖脂）和福斯曼抗原（绵羊红细胞中的主要糖脂）的膜定位。人红细胞血影的短暂胰蛋白酶消化显着聚集了膜内颗粒，并允许标记球苷，其以簇状排列出现。铁蛋白-抗球苷的聚集体与铁蛋白-麦芽凝集素（糖蛋白的标记物）的聚集体不同，后者与膜内颗粒的聚集体相对应。用抗球糖苷/葡萄球菌蛋白A-胶体金和铁蛋白-麦芽凝集素对人胰蛋白酶化的鬼进行双重标记，表明标记模式不同，并且球糖苷的聚集体与代表跨膜蛋白的膜内颗粒没有直接关系。用铁蛋白缀合的兔抗福斯曼抗体标记的重新密封的绵羊红细胞鬼影在红细胞表面上显示出小簇的福斯曼糖脂，其可以与第二种山羊抗兔抗体明显聚集，表明小糖脂结构域的相对流动性。在pH 5.5处理以聚集膜内颗粒的羊鬼中，铁蛋白-抗-福斯曼标记的分布也没有显示出膜内颗粒与铁蛋白-抗-福斯曼簇之间的明确对应关系。
Using the freeze-etch technique, the membrane localization of globoside, a principal glycolipid in human erythrocytes, and Forssman antigen, the chief glycolipid in sheep erythrocytes was evaluated using ferritin and colloidal gold as morphological markers for rabbit antibodies prepared against these glycolipids. Brief trypsinization of human red cell ghosts markedly aggregated intramembranous particles and permitted labeling of globoside, which appeared in a clustered arrangement. The aggregates of ferritin-anti-globoside differed from those of ferritin-wheat germ agglutinin, a label for glycophorin, which corresponded with the aggregates of intramembranous particles. Double-labeling of human trypsinized ghosts with anti-globoside/Staphylococcalprotein A-colloidal gold and ferritin-wheat germ agglutinin indicated that the patterns of labeling were different and that the aggregates of globoside did not bear a direct relationship to the intramembranous particles, which represent transmembrane proteins. Resealed sheep erythrocyte ghosts labeled with ferritin-conjugated rabbit anti-Forssman showed small clusters of Forssman glycolipid on the erythrocyte surface, which could be markedly aggregated with a second goat anti-rabbit antibody, indicating relative mobility of the small glycolipid domains. The distribution of ferritin-anti-Forssman label in sheep ghosts treated at pH 5.5 to aggregate intramembranous particles also did not show definite correspondence between intramembranous particles and the clusters of ferritin-anti-Forssman.