Kramer R H, Canellakis E S
Biochim Biophys Acta. 1979 Mar 8;551(2):328-48. doi: 10.1016/0005-2736(89)90010-2.
The sensitivity of 125I-labeled sialoglycoproteins to neuraminidase digestion was used to monitor the loss of specific membrane glycoproteins from the cell surface in to the cytoplasmic compartment during lectin-mediated endocytosis. These studies demonstrated that a major portion of the surface glycoproteins had undergone internalization concurrently with wheat germ agglutinin in a time- and temperature-dependent process. The internalized 125I-labeled glycoproteins were associated with the small vesicle fraction and were present in the same relative proportion as they existed in the plasma membrane isolated from control untreated cells. Many of the 125I-labeled membrane proteins were shown to be receptors and were isolated after affinity chromatography of the solubilized plasma membranes on wheat germ agglutinin-agarose columns.
利用125I标记的唾液酸糖蛋白对神经氨酸酶消化的敏感性,来监测在凝集素介导的内吞作用过程中,特定膜糖蛋白从细胞表面向细胞质区室的丢失情况。这些研究表明,大部分表面糖蛋白在一个时间和温度依赖性过程中,与麦胚凝集素同时发生了内化。内化的125I标记糖蛋白与小囊泡部分相关,并且其相对比例与从未经处理的对照细胞分离的质膜中的比例相同。许多125I标记的膜蛋白被证明是受体,并且在将溶解的质膜在麦胚凝集素-琼脂糖柱上进行亲和层析后被分离出来。