Davis L I, Blobel G
Cell. 1986 Jun 6;45(5):699-709. doi: 10.1016/0092-8674(86)90784-1.
We describe studies using a monoclonal antibody that recognizes a 62 kd protein (p62) of rat liver nuclei. This protein remains associated with the nuclear pore complex-lamina fraction resulting from treatment of nuclei with DNAase, RNAase, and nonionic detergent. Immunofluorescence revealed a strikingly punctate pattern of nuclear rim staining. By immunoferritin microscopy, p62 was specifically localized to the pore complex. Thus, pore complexes can be resolved by fluorescence light microscopy. Pulse chase analysis of labeled tissue culture cells showed that p62 is synthesized as a soluble cytoplasmic precursor of 61 kd, which is incorporated into the nuclear fraction with an unusually long t1/2 of about 6 hr. Incorporation is followed by modification that may involve addition of N-acetylglucosamine residues.
我们描述了使用一种单克隆抗体进行的研究，该抗体可识别大鼠肝细胞核的一种62kd蛋白（p62）。在用DNA酶、RNA酶和非离子去污剂处理细胞核后，这种蛋白质仍与核孔复合体-核纤层部分相关联。免疫荧光显示核边缘染色呈现出显著的点状模式。通过免疫铁蛋白显微镜观察，p62特异性定位于孔复合体。因此，孔复合体可以通过荧光显微镜分辨出来。对标记组织培养细胞的脉冲追踪分析表明，p62作为一种61kd的可溶性细胞质前体合成，其以约6小时的异常长的半衰期掺入核部分。掺入后会发生修饰，可能涉及添加N-乙酰葡糖胺残基。
