Thomson J A, Chiu J F, Sakuma K, Hnilica L S
Cancer Res. 1977 Sep;37(9):3266-73.
Protein phosphokinases were isolated from the nuclei of normal and fetal liver and neoplastic tissues. Chromatography on phosphocellulose columns resolved the normal and fetal liver kinases into five reproducible fractions. Each of the fractions differed in optimal divalent cation and substrate requirements. Hepatic proliferation was accompanied by quantitative changes in the kinase activity profiles (with endogenous phosphoprotein as natural substrate). An additional phosphoprotein kinase activity stimulated by Mn2+ was found in the nuclei of malignant cells. This tumor-specific kinase could not be detected either in tumor cytoplasm or in fetal or regenerating liver nuclei. Mn2+-dependent phosphoprotein kinase from Novikoff hepatoma phosphorylated only one major protein band detectable by polyacrylamide gel electrophoresis. This substrate could not be detected in chromatin of normal tissues.
从正常肝脏、胎儿肝脏及肿瘤组织的细胞核中分离出了蛋白质磷酸激酶。在磷酸纤维素柱上进行色谱分析，可将正常肝脏和胎儿肝脏的激酶分离成五个可重复的组分。每个组分在最佳二价阳离子和底物需求方面都有所不同。肝脏增殖伴随着激酶活性谱的定量变化（以内源性磷蛋白作为天然底物）。在恶性细胞的细胞核中发现了一种受锰离子刺激的额外磷蛋白激酶活性。在肿瘤细胞质或胎儿或再生肝脏细胞核中均未检测到这种肿瘤特异性激酶。来自诺维科夫肝癌的锰离子依赖性磷蛋白激酶仅使聚丙烯酰胺凝胶电泳可检测到的一条主要蛋白带发生磷酸化。在正常组织的染色质中未检测到这种底物。
