PMID- 7654865
OWN - NLM
STAT- MEDLINE
DCOM- 19951002
LR  - 20211203
IS  - 0320-9725 (Print)
IS  - 0320-9725 (Linking)
VI  - 60
IP  - 6
DP  - 1995 Jun
TI  - [Effect of polyanions on the structure of rat liver nuclear chromatin].
PG  - 905-16
AB  - Stepwise addition of polyanions (PA)-heparin and dextran sulfate-to interphase 
      rat liver nuclei results in increased chromatin condensation (PA/DNA = 0.125) 
      followed by its decondensation down to 10 nm fibrils (PA/DNA = 0.2) and, 
      eventually, (PA/DNA > 0.3) to a new condensation of the material up to 30-50 nm 
      fibrils and 0.15-0.5 M compact globular particles (GP). After subsequent addition 
      of ammonium acetate (0.15-0.5 M) the whole nuclear material converts into an even 
      network of GP connected by fibrils containing DNA. The GP diameter (40-70 nm) is 
      unaffected in the PA/DNA range of 0.4 to 1.5. The GP-containing nuclei retain up 
      to 85-90% of DNA and 50-70% of the protein. Treatment of the nuclei with 
      staphylococcal nuclease reveals the absence of nucleosomal periodicity in the DNA 
      structure. The nuclei treated with PA and the salt in the presence of EDTA retain 
      all the histones of the nucleosomal core. When treated in the presence of Mg2+, 
      the nuclei retain also histone H1. The GP obtained at pH 6.0-6.5 are the most 
      compact ones. At pH 5.0 and 8.5 GP partly form tangles of approximately 10 nm 
      granules linked by thin fibrils. GP can be reversibly unfolded into the same 
      fibro-granular network when dyalized against low ionic strength solutions in the 
      presence of EDTA. A more than 1.5-fold increase in the PA/DNA ratio or treatment 
      of GP-containing nuclei with nucleases terminate in the failure of the fibrillar 
      network between GP, giving rise to large globules (> 300 nm), presumably at the 
      expense of GP fusion. In this case the nuclei lose DNA but retain no less than 
      70% of histones. The diameter of large globules depends on the concentration of 
      PA. GP are suggested to arise by the aggregation of PA complexes with histone 
      cores of nucleosomes and with other alkaline proteins of chromatin at the 
      regularly spaced sites of partly deproteinated chromatin.
FAU - Prusov, A N
AU  - Prusov AN
LA  - rus
PT  - Journal Article
TT  - Deistvie polianionov na strukturu khromatina iader pecheni krysy.
PL  - Russia (Federation)
TA  - Biokhimiia
JT  - Biokhimiia (Moscow, Russia)
JID - 0372667
RN  - 0 (Chromatin)
RN  - 0 (Polyelectrolytes)
RN  - 0 (Polymers)
RN  - 0 (polyanions)
RN  - I38ZP9992A (Magnesium)
SB  - IM
MH  - Animals
MH  - Cell Nucleus/*drug effects/metabolism
MH  - Chromatin/chemistry/*metabolism
MH  - Hydrogen-Ion Concentration
MH  - Liver/*drug effects/metabolism/ultrastructure
MH  - Magnesium/chemistry
MH  - Polyelectrolytes
MH  - Polymers/*pharmacology
MH  - Protein Conformation
MH  - Protein Folding
MH  - Rats
EDAT- 1995/06/01 00:00
MHDA- 1995/06/01 00:01
CRDT- 1995/06/01 00:00
PHST- 1995/06/01 00:00 [pubmed]
PHST- 1995/06/01 00:01 [medline]
PHST- 1995/06/01 00:00 [entrez]
PST - ppublish
SO  - Biokhimiia. 1995 Jun;60(6):905-16.