Newmeyer D D, Ohlsson-Wilhelm B M
Chromosoma. 1985;92(4):297-303. doi: 10.1007/BF00329813.
We report here the isolation of a monoclonal antibody, J17, that reacts with a conserved vertebrate protein antigen that is present in the spindle apparatus during mitosis but found within the nucleus during interphase. Immunofluorescence microscopy demonstrates that the J17 antigen is found in numerous punctate regions that are distinct from nucleoli. Furthermore, this antigen is not directly associated with kinetochores, the nuclear envelope, or with metaphase chromosomes. Antibody J17 immunoprecipitates a single polypeptide of very high molecular weight (over 250 000) from K562 human erythroleukemia cells pulse-labeled with 14C-leucine. This polypeptide is converted quantitatively to a stable 220-kilodalton product within one cellular generation. We discuss the possible relevance of this processing event for transport into the nucleus. The J17 antigen is synthesized throughout the cell cycle in Chinese hamster ovary cells.
我们在此报告一种单克隆抗体J17的分离情况，该抗体可与一种保守的脊椎动物蛋白抗原发生反应，这种抗原在有丝分裂期间存在于纺锤体中，但在间期存在于细胞核内。免疫荧光显微镜检查表明，J17抗原存在于许多与核仁不同的点状区域。此外，该抗原与动粒、核膜或中期染色体无直接关联。抗体J17从用¹⁴C - 亮氨酸脉冲标记的K562人红白血病细胞中免疫沉淀出一种分子量非常高（超过250 000）的单一多肽。在一个细胞世代内，这种多肽定量转化为一种稳定的220千道尔顿产物。我们讨论了这种加工事件与转运入核的可能相关性。J17抗原在中华仓鼠卵巢细胞的整个细胞周期中都有合成。
