[Stability of DNA-protein interactions in chromatin fractions with different sensitivity to nucleases].
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.
S''iakste
N I
NI
Budylin
A V
AV
D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000378:metabolism; D002843:Chromatin / Q000378:metabolism*; D004706:Endodeoxyribonucleases / Q000378:metabolism*; D051379:Mice; D008836:Micrococcal Nuclease / Q000378:metabolism*; D009698:Nucleoproteins / Q000378:metabolism*
D002843:Chromatin; D009698:Nucleoproteins; D004706:Endodeoxyribonucleases; C019329:deoxyribonuclease II; D008836:Micrococcal Nuclease
Prochnost' DNK-belkovykh vzaimodeĭstviĭ v razlichaiushchikhsia po chuvstvitel'nosti k nukleazam fraktsiiam khromatina.