Dilworth S M
CRC Molecular Embryology Research Group, Department of Zoology, Cambridge, UK.
J Cell Sci. 1991 Mar;98 ( Pt 3):309-15. doi: 10.1242/jcs.98.3.309.
An antibody that recognizes the phosphorylated form of nucleoplasmin has identified another nuclear protein whose antigenic form is regulated in a mitosis-specific manner, with a dramatic increase in binding occurring in all mitotic cells. The protein is localised around the periphery of condensed chromosomes during mitosis in a manner analogous to another nucleoplasmin-related polypeptide NO38. Mitosis-specific expression of the antigenic site is dependent on phosphorylation of the polypeptide; binding of the antibody is dramatically reduced by prior incubation of the polypeptide with phosphatases. Migration on SDS-PAGE suggests that the protein has an exceptionally large relative molecular mass, in excess of 400,000. The probable mitosis-specific phosphorylation and location of this antigen suggests a subcellular storage mechanism for proteins during mitosis.
一种识别核质蛋白磷酸化形式的抗体鉴定出了另一种核蛋白,其抗原形式以有丝分裂特异性方式受到调控,在所有有丝分裂细胞中结合显著增加。该蛋白在有丝分裂期间定位于浓缩染色体的周边,其方式类似于另一种与核质蛋白相关的多肽NO38。抗原位点的有丝分裂特异性表达取决于该多肽的磷酸化;在多肽与磷酸酶预先孵育后,抗体的结合显著减少。在SDS-PAGE上的迁移表明该蛋白具有异常大的相对分子质量,超过400,000。这种抗原可能的有丝分裂特异性磷酸化和定位提示了有丝分裂期间蛋白质的亚细胞储存机制。