Eagles P A, Johnson L N, Van Horn C
J Cell Sci. 1975 Oct;19(1):33-54. doi: 10.1242/jcs.19.1.33.
The distribution of concanavalin A (con A) receptor sites on the membranes of chromaffin granules has been investigated by binding studies using 125I-labelled con A and by electron-microscope studies using ferritin-labelled con A. In both experiments con A was observed to bind to chromaffin granule membranes but not to intact granules. The ferritin-con A particles bind to only one of the two possible surfaces of the chromaffin granule membranes. These results are in agreement with previous observations concerning the asymmetric distribution of saccharide residues on the surfaces of a number of different plasma membranes. They suggest that for the intracellular membrane of the chromaffin granule the saccharide sites, like those in plasma membranes, are not exposed to the cell cytoplasm. Further work is necessary to establish whether these sites are on the inner surface of the membrane or whether they are unmasked during the conversion of granules to membrane ghosts.
已通过使用¹²⁵I标记的伴刀豆球蛋白A(伴刀豆球蛋白A)的结合研究以及使用铁蛋白标记的伴刀豆球蛋白A的电子显微镜研究,对嗜铬颗粒膜上伴刀豆球蛋白A(伴刀豆球蛋白A)受体位点的分布进行了研究。在这两个实验中,均观察到伴刀豆球蛋白A与嗜铬颗粒膜结合,但不与完整颗粒结合。铁蛋白-伴刀豆球蛋白A颗粒仅与嗜铬颗粒膜两个可能表面中的一个结合。这些结果与先前关于许多不同质膜表面糖残基不对称分布的观察结果一致。它们表明,对于嗜铬颗粒的细胞内膜,糖位点与质膜中的糖位点一样,不暴露于细胞质。需要进一步的工作来确定这些位点是在膜的内表面上,还是在颗粒转化为膜空壳的过程中被暴露出来。