S''iakste N I, Budylin A V
Mol Gen Mikrobiol Virusol. 1988 Oct(10):30-4.
It was revealed by means of nucleoprotein-celite-chromatography that DNA-protein interactions in the chromatin fraction sensitive to micrococcal nuclease and DNase II are weaker that in the resistant one. The micrococcal nuclease destroys the DNA-matrix bond resistant to salt-urea, while DNase II does not change the DNA-matrix integrity. Tightness of the DNA-protein interactions is weakened by the increasing chromatin fragmentation, but does not depend on the size of chromatin particles.
通过核蛋白-硅藻土色谱法揭示,对微球菌核酸酶和DNase II敏感的染色质组分中的DNA-蛋白质相互作用比抗性组分中的弱。微球菌核酸酶破坏对盐-尿素有抗性的DNA-基质键,而DNase II不会改变DNA-基质的完整性。DNA-蛋白质相互作用的紧密性会随着染色质片段化程度的增加而减弱,但不取决于染色质颗粒的大小。