Gabrielli F, Courtneidge S A
Differentiation Programme, European Molecular Biology Laboratory, Heidelberg, Germany.
Ital J Biochem. 1992 Jan-Feb;41(1):9-15.
Normal (Rat 1) and transformed cells (middle T antigen-transformed derivative 3C3) were grown in the presence of 32P-orthophosphate. 32P-labelled nuclear proteins were fractionated by means of two-dimensional gel electrophoresis and detected by autoradiography. The comparative analysis of the autoradiographs of the normal and transformed cells revealed differences in the phosphorylation patterns of histone and low-molecular-mass high mobility group proteins (HMG). Three of the HMG proteins were highly phosphorylated in the transformed cells, and the analysis of their phosphorylation sites showed that these HMG proteins were phosphorylated on serine and threonine but not on tyrosine residues.
正常细胞（大鼠1）和转化细胞（中T抗原转化的衍生物3C3）在32P-正磷酸盐存在的情况下生长。通过二维凝胶电泳对32P标记的核蛋白进行分级分离，并通过放射自显影进行检测。对正常细胞和转化细胞放射自显影片的比较分析揭示了组蛋白和低分子量高迁移率族蛋白（HMG）磷酸化模式的差异。其中三种HMG蛋白在转化细胞中高度磷酸化，对其磷酸化位点的分析表明，这些HMG蛋白在丝氨酸和苏氨酸上磷酸化，而在酪氨酸残基上未磷酸化。
