Foxwell B M, Tanner M J
Biochem J. 1981 Apr 1;195(1):129-37. doi: 10.1042/bj1950129.
We studied the surfaces of maturing rabbit bone-marrow erythroid cells for the presence of the erythrocyte anion-transport protein by using an immunochemical method. An antibody was raised against the purified anion-transport protein. The antibody was shown to react specifically with the anion-transport protein and it recognized determinants in the extracellular as well as the cytoplasmic or intramembranous domains of the protein. The binding of the antibody to the surface of intact rabbit bone-marrow erythroid cells was studied by using the Staphylococcus aureus 'rosette' technique described by Gahmberg, Jokinen & Andersson [(1978) Blood 52, 379-386]. Although pronormoblasts had little of the protein, there was a progressive increase in the amount of the protein at the surface of cells of increasing maturity up to the reticulocyte stage. Most of the protein is inserted into the plasma membrane between the polychromatic-normoblast and reticulocyte stage of the cell.
我们采用免疫化学方法研究了成熟兔骨髓红系细胞表面是否存在红细胞阴离子转运蛋白。制备了针对纯化的阴离子转运蛋白的抗体。该抗体被证明能与阴离子转运蛋白特异性反应，并且能识别该蛋白细胞外以及细胞质或膜内区域的决定簇。利用Gahmberg、Jokinen和Andersson [（1978年）《血液》52卷，379 - 386页]所描述的金黄色葡萄球菌“花环”技术，研究了抗体与完整兔骨髓红系细胞表面的结合情况。尽管原成红细胞几乎不含该蛋白，但在细胞成熟度不断增加直至网织红细胞阶段的过程中，细胞表面该蛋白的量逐渐增加。大部分蛋白是在细胞从多染性成红细胞阶段到网织红细胞阶段之间插入质膜的。
