Casadei J M, Barchi R L
J Neurochem. 1987 Mar;48(3):773-8. doi: 10.1111/j.1471-4159.1987.tb05584.x.
Twenty-one monoclonal antibodies specific for the rat skeletal muscle voltage-sensitive sodium channel have been characterized according to subunit reactivity, recognition of carbohydrates, and mutual binding interactions. All antibodies recognize the 260-kDa alpha-subunit of the sodium channel on immunoblots. N-Acetylneuraminic acid inhibited the binding of five antibodies in a concentration-dependent manner, but five other monosaccharides known to be components of the channel had no effect on antibody binding. Competition studies using biosynthetically labeled antibodies separated these 21 antibodies into groups recognizing at least nine distinct domains. Through common interactions between domains, these could in turn be associated into two larger topologically related regions. One region encompasses seven interacting domains and 16 antibodies. This region is probably extracellular by virtue of the interaction of one subgroup with N-acetylneuraminic acid, and may represent a particularly immunogenic region on this channel protein.
根据亚基反应性、对碳水化合物的识别以及相互结合相互作用，对21种针对大鼠骨骼肌电压门控钠通道的单克隆抗体进行了表征。所有抗体在免疫印迹中均识别钠通道的260 kDaα亚基。N-乙酰神经氨酸以浓度依赖的方式抑制了五种抗体的结合，但已知是通道组成成分的其他五种单糖对抗体结合没有影响。使用生物合成标记抗体的竞争研究将这21种抗体分为识别至少九个不同结构域的组。通过结构域之间的共同相互作用，这些结构域又可关联成两个更大的拓扑相关区域。一个区域包含七个相互作用的结构域和16种抗体。由于一个亚组与N-乙酰神经氨酸相互作用，该区域可能位于细胞外，并且可能代表该通道蛋白上一个特别具有免疫原性的区域。
