Vorbrodt A, Maul G G
J Histochem Cytochem. 1980 Jan;28(1):27-35. doi: 10.1177/28.1.6153190.
Cytochemical tests for nucleosidetriphosphatase (NTPase) and Bernhard's preferential staining for ribonucleoproteins (RNP) were applied to isolated rat liver nuclei. The strongest and most easily reproducible positive reaction for NTPase was detected at pH 7.7 with ATP and GTP. This reaction was activated by Mg2+ and Ca2+ and inhibited by Be2+, Zn2+, quercetin, and ribonuclease. The major sites of enzyme reaction were intranuclear RNA-containing structures. Incubation of nuclei in ATP-stimulated RNA-release medium eliminated a considerable part of the material showing both NTPase reaction and staining for RNP; the perichromatin granules disappeared, while interchromatin granules remained. NTPase activity in the nuclear envelope seems to be associated with the annular part of nuclear pore complexes (permanent component) and with RNP particles translocated through nuclear pores or attached to the surface of nuclei (transitional component). From a morphological point of view, these observations support previous biochemical data suggesting the existence of a connection between NTPase activity and the translocation of RNP particles through the nuclear envelope.
对分离出的大鼠肝细胞核进行了核苷三磷酸酶（NTPase）的细胞化学测试以及伯恩哈德对核糖核蛋白（RNP）的优先染色。在pH 7.7条件下，使用ATP和GTP时，检测到了最强且最易于重复的NTPase阳性反应。该反应被Mg2+和Ca2+激活，被Be2+、Zn2+、槲皮素和核糖核酸酶抑制。酶反应的主要部位是核内含有RNA的结构。将细胞核置于ATP刺激的RNA释放培养基中孵育，消除了相当一部分同时显示NTPase反应和RNP染色的物质；核周染色质颗粒消失，而染色质间颗粒仍然存在。核膜中的NTPase活性似乎与核孔复合体的环形部分（永久成分）以及通过核孔转运或附着在核表面的RNP颗粒（过渡成分）有关。从形态学角度来看，这些观察结果支持了先前的生化数据，表明NTPase活性与RNP颗粒通过核膜的转运之间存在联系。
